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2024-04-20 16:21:19, GGRNA : RefSeq release 60 (20130726)
LOCUS NM_001134418 3082 bp mRNA linear PRI 17-APR-2013
DEFINITION Homo sapiens leprecan-like 1 (LEPREL1), transcript variant 2, mRNA.
ACCESSION NM_001134418
VERSION NM_001134418.1 GI:197313661
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (bases 1 to 3082)
AUTHORS Mordechai,S., Gradstein,L., Pasanen,A., Ofir,R., El Amour,K.,
Levy,J., Belfair,N., Lifshitz,T., Joshua,S., Narkis,G.,
Elbedour,K., Myllyharju,J. and Birk,O.S.
TITLE High myopia caused by a mutation in LEPREL1, encoding prolyl
3-hydroxylase 2
JOURNAL Am. J. Hum. Genet. 89 (3), 438-445 (2011)
PUBMED 21885030
REMARK GeneRIF: High myopia is caused by a mutation in LEPREL1, encoding
prolyl 3-hydroxylase 2.
REFERENCE 2 (bases 1 to 3082)
AUTHORS Fernandes,R.J., Farnand,A.W., Traeger,G.R., Weis,M.A. and Eyre,D.R.
TITLE A role for prolyl 3-hydroxylase 2 in post-translational
modification of fibril-forming collagens
JOURNAL J. Biol. Chem. 286 (35), 30662-30669 (2011)
PUBMED 21757687
REMARK GeneRIF: P3H2 has preferred substrate sequences among the classes
of 3Hyp sites in clade A collagen chains
REFERENCE 3 (bases 1 to 3082)
AUTHORS Shah,R., Smith,P., Purdie,C., Quinlan,P., Baker,L., Aman,P.,
Thompson,A.M. and Crook,T.
TITLE The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for
epigenetic silencing in breast cancer
JOURNAL Br. J. Cancer 100 (10), 1687-1696 (2009)
PUBMED 19436308
REMARK GeneRIF: The restriction of silencing in P3H2 to breast carcinomas,
and its association with oestrogen-receptor-positive cases,
suggests that P3H2 may be a breast-cancer-specific tumour
suppressor.
REFERENCE 4 (bases 1 to 3082)
AUTHORS Tiainen,P., Pasanen,A., Sormunen,R. and Myllyharju,J.
TITLE Characterization of recombinant human prolyl 3-hydroxylase
isoenzyme 2, an enzyme modifying the basement membrane collagen IV
JOURNAL J. Biol. Chem. 283 (28), 19432-19439 (2008)
PUBMED 18487197
REMARK GeneRIF: P3H2 is responsible for the hydroxylation of collagen IV,
which has the highest 3-hydroxyproline content of all collagens. It
is thus possible that P3H2 mutations may lead to a disease with
changes in basement membranes.
REFERENCE 5 (bases 1 to 3082)
AUTHORS Vranka,J.A., Sakai,L.Y. and Bachinger,H.P.
TITLE Prolyl 3-hydroxylase 1, enzyme characterization and identification
of a novel family of enzymes
JOURNAL J. Biol. Chem. 279 (22), 23615-23621 (2004)
PUBMED 15044469
REFERENCE 6 (bases 1 to 3082)
AUTHORS Jarnum,S., Kjellman,C., Darabi,A., Nilsson,I., Edvardsen,K. and
Aman,P.
TITLE LEPREL1, a novel ER and Golgi resident member of the Leprecan
family
JOURNAL Biochem. Biophys. Res. Commun. 317 (2), 342-351 (2004)
PUBMED 15063763
REFERENCE 7 (bases 1 to 3082)
AUTHORS Thelin-Jarnum,S., Lassen,C., Panagopoulos,I., Mandahl,N. and
Aman,P.
TITLE Identification of genes differentially expressed in TLS-CHOP
carrying myxoid liposarcomas
JOURNAL Int. J. Cancer 83 (1), 30-33 (1999)
PUBMED 10449603
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from DA720646.1, BC005029.1,
AC016966.19, BU621129.1 and BU737886.1.
This sequence is a reference standard in the RefSeqGene project.
Summary: This gene encodes a member of the prolyl 3-hydroxylase
subfamily of 2-oxo-glutarate-dependent dioxygenases. These enzymes
play a critical role in collagen chain assembly, stability and
cross-linking by catalyzing post-translational 3-hydroxylation of
proline residues. Mutations in this gene are associated with
nonsyndromic severe myopia with cataract and vitreoretinal
degeneration, and downregulation of this gene may play a role in
breast cancer. Alternatively spliced transcript variants encoding
multiple isoforms have been observed for this gene. [provided by
RefSeq, Dec 2011].
Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
portion of the 5' coding region and initiates translation at a
downstream, in-frame start codon, compared to variant 1. The
encoded isoform (b) has a shorter N-terminus, compared to isoform
a.
##Evidence-Data-START##
Transcript exon combination :: BC005029.1 [ECO:0000332]
RNAseq introns :: mixed/partial sample support
ERS025081, ERS025082 [ECO:0000350]
##Evidence-Data-END##
COMPLETENESS: complete on the 3' end.
PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP
1-172 DA720646.1 1-172
173-450 BC005029.1 1-278
451-451 AC016966.19 36592-36592 c
452-2346 BC005029.1 280-2174
2347-2963 BU621129.1 17-633 c
2964-3082 BU737886.1 1-119 c
FEATURES Location/Qualifiers
source 1..3082
/organism="Homo sapiens"
/mol_type="mRNA"
/db_xref="taxon:9606"
/chromosome="3"
/map="3q28"
gene 1..3082
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/note="leprecan-like 1"
/db_xref="GeneID:55214"
/db_xref="HGNC:19317"
/db_xref="MIM:610341"
exon 1..235
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
misc_feature 224..226
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/note="upstream in-frame stop codon"
exon 236..388
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
CDS 299..1882
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/EC_number="1.14.11.7"
/note="isoform b is encoded by transcript variant 2;
prolyl 3-hydroxylase 3; prolyl 3-hydroxylase 2; myxoid
liposarcoma-associated protein 4"
/codon_start=1
/product="prolyl 3-hydroxylase 2 isoform b"
/protein_id="NP_001127890.1"
/db_xref="GI:197313662"
/db_xref="CCDS:CCDS46981.1"
/db_xref="GeneID:55214"
/db_xref="HGNC:19317"
/db_xref="MIM:610341"
/translation="
MEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREYFVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSPIENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPASIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGAEVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELHSVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARRIVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAYTFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKGKRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
"
misc_feature 1169..1765
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/note="Prolyl 4-hydroxylase alpha subunit homologues;
Region: P4Hc; smart00702"
/db_xref="CDD:197834"
misc_feature 1484..1765
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/note="2OG-Fe(II) oxygenase superfamily; Region:
2OG-FeII_Oxy_3; pfam13640"
/db_xref="CDD:205817"
variation 367
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="c"
/replace="t"
/db_xref="dbSNP:34128856"
exon 389..578
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 451
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="c"
/replace="t"
/db_xref="dbSNP:1719600"
exon 579..710
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
exon 711..853
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 727
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="g"
/db_xref="dbSNP:34558237"
exon 854..943
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 924
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="g"
/db_xref="dbSNP:35904452"
exon 944..984
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 977
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="g"
/db_xref="dbSNP:35737596"
exon 985..1079
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
exon 1080..1207
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 1132
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="g"
/db_xref="dbSNP:35257648"
variation 1207
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="t"
/db_xref="dbSNP:34111865"
exon 1208..1303
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 1263
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="g"
/db_xref="dbSNP:35072845"
exon 1304..1454
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
exon 1455..1572
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 1559
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="c"
/replace="t"
/db_xref="dbSNP:34620268"
variation 1562
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="c"
/db_xref="dbSNP:35067805"
exon 1573..1648
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
exon 1649..1789
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
variation 1762
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/replace="a"
/replace="c"
/db_xref="dbSNP:1061534"
exon 1790..3066
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/inference="alignment:Splign:1.39.8"
STS 2408..2597
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/standard_name="RH93767"
/db_xref="UniSTS:87517"
STS 2573..2714
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
/standard_name="STS-N21495"
/db_xref="UniSTS:21296"
polyA_signal 2941..2946
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
polyA_site 2963
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
polyA_signal 3045..3050
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
polyA_site 3066
/gene="LEPREL1"
/gene_synonym="MCVD; MLAT4; P3H2"
ORIGIN
agaagaccacagaaatgcctccaggaggcaggctgggatccagggtccaaccaatattcttgtgagagtgtgaagccaaggaacacgaaagaggggaacaccttggctaagaatgtattcgtgacagaggagaaggggaggaacaggaagcctccagctagtcgtttggaatctggcaaccatttctgtcagctttctcattcctagattgatgcagattgcttaattccttgagcttaaccagctcgaaaaagcagtggaagcagctcacacatttttcgtggctaaccctgagcacatggaaatgcagcagaacattgagaattacagggcgacagctggtgttgaagcattgcagttggtagacagagaagccaagccacacatggagagttacaatgcaggagttaaacattatgaggctgatgactttgagatggctatcaggcacttcgaacaagccttaagagaatatttcgttgaagatacagaatgccggaccctatgtgaggggcctcagagatttgaagaatatgagtatttagggtataaggctggtctgtatgaagctattgcagatcactacatgcaggtgcttgtttgtcagcatgaatgtgtgagggaacttgccacccgccctggccgcctctctcccatcgagaattttcttcctctgcactatgattacctacagtttgcctactatcgagttggtgagtatgtgaaagccctggagtgtgccaaagcctatcttctatgccatccagatgatgaggatgtcctagacaatgtggattactatgagagtctgctggatgatagcattgacccggcatccattgaggccagagaggatttaacaatgtttgtgaaacgtcataagctggagtctgagctgataaaatcagctgcagaaggtctggggttttcatacactgaaccgaattattggatcagatatggaggacgacaggatgagaatcgggtcccttcaggagtgaacgtagagggagcagaagttcatggattctcaatgggaaaaaagctatcacccaagatagatcgagacctaagagaaggtggtcctctactctatgagaacatcacattcgtctacaactcggagcagctgaacgggactcagcgggttctcctggataacgtcctgtcggaagaacagtgccgggagctccacagcgtggccagtggaatcatgcttgttggtgatggatacagaggaaaaacttcaccccatacacccaatgaaaagtttgaaggtgcaactgtcctgaaagcactcaaatctggttatgaaggtcgagtcccactgaagagcgctcgtctgttttatgacatcagcgaaaaggctcgaaggattgtagaatcttattttatgctgaactcaactctgtatttttcctatacacacatggtctgccgaacagccctgtctggtcagcaggatagaagaaatgacctcagtcatcccatccatgctgacaactgtttgttggatccagaggccaacgaatgctggaaggagcctcctgcttacacatttcgagactatagtgctctcctatatatgaatgatgactttgaaggaggagaattcatattcacagagatggatgctaagactgtgactgcctctataaaaccaaaatgtgggcgcatgatcagcttctcatctggaggagagaaccctcatggggtgaaggcagtcaccaagggaaagaggtgtgctgtggctctgtggttcaccttggacccactttatagagaattggagcgaatacaggctgatgaagtgattgcaattctggatcaagaacagcaagggaagcatgaactgaatatcaaccctaaagatgagctataaaaatgagaaagaatgttctatcaaatatttatttaaattgttaatcttatgagaacctttttatttttgtacagagccatggtataaattaacaggttaatgtcagtcatcagatcttccttctcttcctaaggatgcttgtgttgcctcaatctatcaatctatctttcttgttttgggttgttttctctctctctctctctctctctcttcttagagacatggtctaaccatgttgtctaggatatagggcagtggctattcacagatgtgatgatagcacactggagcctcaaactcttaggctcaggcgatccttcaagcctcccggggagctgggaccacaggcacgtgccaccacacccagctctctttcttggtttttcatcatttcatgtatctatcaaagcccagttcacctcctcccccaaacacacacacacacacacacacacacacacacacacacaattaagttgctgcaaattcaaaagcttagagagaataagcttcttggtggtgaaactacaactctcacgtgtgctccagttctaaaattaacctgtgcctggtctctgaagccctttcttgctctgtgcctttcagccacatccttaggtgctaacggccatgagctccgactctccaaagtgagctccactttgggtctgaggagcccctggcagagtccacgctgcctcaggtatcatgggcgtaatgatcacccaggctccgggagatctcatggatgattactgtatgagacagaggggacttcagtctttccagggccttggtggaatttttggctctggtgttttcgccagacaataaacttacactggaagctttgattcaccctccacagtactccagaaaggactgtcctataagttgtacactttaaaaggtcatgtagaggttgtagtagaatggcttttcaccctggtgactttggaagaaactcttgaatactgcctgcatccgggcaccatggccaggttgcctaggagtggggtccactgatgaaaagaggtgttttgtacttacataagaaaaataaatttctgattgattttaaccgtcatctgcttatattttgggggcccctcctcattgctgctatccagcacacagatttgtgcttgtgtctgatttgtttaataaagggaggcttattttaaaaaaaaaaaaaaaaaa
//
ANNOTATIONS from NCBI Entrez Gene (20130726):
GeneID:55214 -> Molecular function: GO:0005506 [iron ion binding] evidence: IEA
GeneID:55214 -> Molecular function: GO:0016702 [oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen] evidence: IEA
GeneID:55214 -> Molecular function: GO:0019797 [procollagen-proline 3-dioxygenase activity] evidence: IDA
GeneID:55214 -> Molecular function: GO:0031418 [L-ascorbic acid binding] evidence: IEA
GeneID:55214 -> Biological process: GO:0008285 [negative regulation of cell proliferation] evidence: IDA
GeneID:55214 -> Biological process: GO:0019511 [peptidyl-proline hydroxylation] evidence: IDA
GeneID:55214 -> Biological process: GO:0030198 [extracellular matrix organization] evidence: TAS
GeneID:55214 -> Biological process: GO:0032963 [collagen metabolic process] evidence: IDA
GeneID:55214 -> Cellular component: GO:0005604 [basement membrane] evidence: ISS
GeneID:55214 -> Cellular component: GO:0005783 [endoplasmic reticulum] evidence: IDA
GeneID:55214 -> Cellular component: GO:0005788 [endoplasmic reticulum lumen] evidence: TAS
GeneID:55214 -> Cellular component: GO:0005794 [Golgi apparatus] evidence: IDA
ANNOTATIONS from NCBI Entrez Gene (20130726):
NP_001127890 -> EC 1.14.11.7
by
@meso_cacase at
DBCLS
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