P3H1_HUMAN
ID P3H1_HUMAN Reviewed; 736 AA.
AC Q32P28; Q7KZR4; Q96BR8; Q96SK8; Q96SL5; Q96SN3; Q9H6K3; Q9HC86; Q9HC87;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Prolyl 3-hydroxylase 1 {ECO:0000312|HGNC:HGNC:19316};
DE EC=1.14.11.7;
DE AltName: Full=Growth suppressor 1 {ECO:0000303|PubMed:10951563};
DE AltName: Full=Leucine- and proline-enriched proteoglycan 1 {ECO:0000250|UniProtKB:Q9R1J8};
DE Short=Leprecan-1 {ECO:0000250|UniProtKB:Q9R1J8};
DE Flags: Precursor;
GN Name=P3H1 {ECO:0000312|HGNC:HGNC:19316};
GN Synonyms=GROS1 {ECO:0000303|PubMed:10951563},
GN LEPRE1 {ECO:0000250|UniProtKB:Q9R1J8}; ORFNames=PSEC0109;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=10951563; DOI=10.1038/sj.onc.1203696;
RA Kaul S.C., Sugihara T., Yoshida A., Nomura H., Wadhwa R.;
RT "Gros1, a potential growth suppressor on chromosome 1: its identity to
RT basement membrane-associated proteoglycan, leprecan.";
RL Oncogene 19:3576-3583(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Epithelium, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Duodenum, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 347-736 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INVOLVEMENT IN OI8.
RX PubMed=17277775; DOI=10.1038/ng1968;
RA Cabral W.A., Chang W., Barnes A.M., Weis M., Scott M.A., Leikin S.,
RA Makareeva E., Kuznetsova N.V., Rosenbaum K.N., Tifft C.J., Bulas D.I.,
RA Kozma C., Smith P.A., Eyre D.R., Marini J.C.;
RT "Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone
RT disorder resembling lethal/severe osteogenesis imperfecta.";
RL Nat. Genet. 39:359-365(2007).
RN [7]
RP INVOLVEMENT IN OI8, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING
RP (ISOFORMS 1; 3 AND 4).
RX PubMed=19088120; DOI=10.1136/jmg.2008.062729;
RA Willaert A., Malfait F., Symoens S., Gevaert K., Kayserili H.,
RA Megarbane A., Mortier G., Leroy J.G., Coucke P.J., De Paepe A.;
RT "Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical
RT documentation and identification of the splice form responsible for prolyl
RT 3-hydroxylation.";
RL J. Med. Genet. 46:233-241(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-540.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan
CC (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-
CC translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences
CC in collagens, especially types IV and V. May be involved in the
CC secretory pathway of cells. Has growth suppressive activity in
CC fibroblasts. {ECO:0000269|PubMed:10951563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Note=Secreted into the extracellular matrix as a
CC chondroitin sulfate proteoglycan (CSPG). {ECO:0000269|PubMed:19088120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=GROS1-L, LEPREa, P3H1a;
CC IsoId=Q32P28-1; Sequence=Displayed;
CC Name=2; Synonyms=GROS1-S;
CC IsoId=Q32P28-2; Sequence=VSP_019346, VSP_019347;
CC Name=3; Synonyms=LEPREc;
CC IsoId=Q32P28-3; Sequence=VSP_019348;
CC Name=4; Synonyms=LEPREb, P3H1b;
CC IsoId=Q32P28-4; Sequence=VSP_054864;
CC -!- PTM: O-glycosylated; chondroitin sulfate. {ECO:0000250}.
CC -!- DISEASE: Osteogenesis imperfecta 8 (OI8) [MIM:610915]: A form of
CC osteogenesis imperfecta, a connective tissue disorder characterized by
CC low bone mass, bone fragility and susceptibility to fractures after
CC minimal trauma. Disease severity ranges from very mild forms without
CC fractures to intrauterine fractures and perinatal lethality.
CC Extraskeletal manifestations, which affect a variable number of
CC patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI8 is characterized by disproportionate short stature, severe
CC osteoporosis, shortening of the long bones, white sclerae, a round face
CC and a short barrel-shaped chest. {ECO:0000269|PubMed:17277775,
CC ECO:0000269|PubMed:19088120}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. A splice site mutation
CC leading to the absence of isoform 1 has been reported in 2 OI8
CC patients. Isoform 1 is the only form predicted to be located in the
CC endoplasmic reticulum, which the appropriate location for the catalysis
CC of collagen hydroxylation. These patients show indeed severely reduced
CC COL1A1 hydroxylation (PubMed:19088120). {ECO:0000269|PubMed:19088120}.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15309.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15256.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC Note=Prolyl 3-hydroxylase 1 (LEPRE1);
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=LEPRE1";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF097431; AAG31018.1; -; mRNA.
DR EMBL; AF097432; AAG31019.1; -; mRNA.
DR EMBL; AK025841; BAB15256.1; ALT_INIT; mRNA.
DR EMBL; AK027648; BAB55264.1; -; mRNA.
DR EMBL; AK027680; BAB55291.1; -; mRNA.
DR EMBL; AK027697; BAB55305.1; -; mRNA.
DR EMBL; AK075418; BAC11608.1; -; mRNA.
DR EMBL; BC015309; AAH15309.2; ALT_INIT; mRNA.
DR EMBL; BC108311; AAI08312.1; -; mRNA.
DR EMBL; BT007039; AAP35688.1; -; mRNA.
DR CCDS; CCDS472.2; -. [Q32P28-1]
DR CCDS; CCDS53307.1; -. [Q32P28-4]
DR CCDS; CCDS57986.1; -. [Q32P28-3]
DR RefSeq; NP_001139761.1; NM_001146289.1. [Q32P28-4]
DR RefSeq; NP_001230175.1; NM_001243246.1. [Q32P28-3]
DR RefSeq; NP_071751.3; NM_022356.3. [Q32P28-1]
DR AlphaFoldDB; Q32P28; -.
DR SMR; Q32P28; -.
DR BioGRID; 122098; 178.
DR IntAct; Q32P28; 47.
DR MINT; Q32P28; -.
DR STRING; 9606.ENSP00000236040; -.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB00172; Proline.
DR DrugBank; DB00139; Succinic acid.
DR GlyConnect; 1639; 10 N-Linked glycans (2 sites).
DR GlyGen; Q32P28; 6 sites, 10 N-linked glycans (2 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; Q32P28; -.
DR MetOSite; Q32P28; -.
DR PhosphoSitePlus; Q32P28; -.
DR BioMuta; P3H1; -.
DR DMDM; 109892809; -.
DR EPD; Q32P28; -.
DR jPOST; Q32P28; -.
DR MassIVE; Q32P28; -.
DR MaxQB; Q32P28; -.
DR PaxDb; Q32P28; -.
DR PeptideAtlas; Q32P28; -.
DR PRIDE; Q32P28; -.
DR ProteomicsDB; 61620; -. [Q32P28-1]
DR ProteomicsDB; 61621; -. [Q32P28-2]
DR ProteomicsDB; 61622; -. [Q32P28-3]
DR Antibodypedia; 32239; 305 antibodies from 23 providers.
DR DNASU; 64175; -.
DR Ensembl; ENST00000236040.8; ENSP00000236040.4; ENSG00000117385.16. [Q32P28-3]
DR Ensembl; ENST00000296388.10; ENSP00000296388.5; ENSG00000117385.16. [Q32P28-1]
DR Ensembl; ENST00000397054.7; ENSP00000380245.3; ENSG00000117385.16. [Q32P28-4]
DR GeneID; 64175; -.
DR KEGG; hsa:64175; -.
DR MANE-Select; ENST00000296388.10; ENSP00000296388.5; NM_022356.4; NP_071751.3.
DR UCSC; uc001chv.3; human. [Q32P28-1]
DR CTD; 64175; -.
DR DisGeNET; 64175; -.
DR GeneCards; P3H1; -.
DR HGNC; HGNC:19316; P3H1.
DR HPA; ENSG00000117385; Low tissue specificity.
DR MalaCards; P3H1; -.
DR MIM; 610339; gene.
DR MIM; 610915; phenotype.
DR neXtProt; NX_Q32P28; -.
DR OpenTargets; ENSG00000117385; -.
DR Orphanet; 216804; Osteogenesis imperfecta type 2.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR PharmGKB; PA134930599; -.
DR VEuPathDB; HostDB:ENSG00000117385; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000158725; -.
DR HOGENOM; CLU_017820_0_0_1; -.
DR InParanoid; Q32P28; -.
DR OMA; HTPSEMF; -.
DR OrthoDB; 660619at2759; -.
DR PhylomeDB; Q32P28; -.
DR TreeFam; TF320837; -.
DR BioCyc; MetaCyc:HS04122-MON; -.
DR BRENDA; 1.14.11.28; 2681.
DR BRENDA; 1.14.11.7; 2681.
DR PathwayCommons; Q32P28; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; Q32P28; -.
DR BioGRID-ORCS; 64175; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; P3H1; human.
DR GenomeRNAi; 64175; -.
DR Pharos; Q32P28; Tbio.
DR PRO; PR:Q32P28; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q32P28; protein.
DR Bgee; ENSG00000117385; Expressed in stromal cell of endometrium and 155 other tissues.
DR ExpressionAtlas; Q32P28; baseline and differential.
DR Genevisible; Q32P28; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:1901874; P:negative regulation of post-translational protein modification; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:ARUK-UCL.
DR GO; GO:0006457; P:protein folding; IMP:UniProtKB.
DR GO; GO:0018126; P:protein hydroxylation; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR039837; P3H1.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14049; PTHR14049; 1.
DR PANTHER; PTHR14049:SF5; PTHR14049:SF5; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Dioxygenase; Dwarfism;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Iron;
KW Metal-binding; Osteogenesis imperfecta; Oxidoreductase; Reference proteome;
KW Repeat; Secreted; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..736
FT /note="Prolyl 3-hydroxylase 1"
FT /id="PRO_0000240352"
FT REPEAT 35..68
FT /note="TPR 1"
FT REPEAT 143..176
FT /note="TPR 2"
FT REPEAT 205..238
FT /note="TPR 3"
FT REPEAT 301..334
FT /note="TPR 4"
FT DOMAIN 564..678
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 699..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..439
FT /evidence="ECO:0000255"
FT MOTIF 733..736
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 708..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 669
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 589
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 659
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 361..363
FT /note="SAK -> QGT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10951563"
FT /id="VSP_019346"
FT VAR_SEQ 364..736
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10951563"
FT /id="VSP_019347"
FT VAR_SEQ 686..736
FT /note="DRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEPAQESLSGSESKPKDEL
FT -> VRAARAGESSWCCGDPFPERPWFAFLFPKSHCQWLRHERSTWDTSSNALSLWSHCL
FT VLPGPAVNGIQVGKEVKTGSDAEFLVPSLGPTSAVLFQRVGPAGKEMSLGPLRNLPCPL
FT GSSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019348"
FT VAR_SEQ 686..736
FT /note="DRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEPAQESLSGSESKPKDEL
FT -> VRAARAGQGAGR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054864"
FT VARIANT 349
FT /note="G -> R (in dbSNP:rs6700677)"
FT /id="VAR_033252"
FT VARIANT 506
FT /note="P -> R (in dbSNP:rs3738501)"
FT /id="VAR_033253"
FT VARIANT 549
FT /note="M -> I (in dbSNP:rs11581921)"
FT /id="VAR_033254"
FT VARIANT 644
FT /note="Q -> K (in dbSNP:rs3738497)"
FT /id="VAR_050442"
FT CONFLICT 102
FT /note="A -> G (in Ref. 1; AAG31018/AAG31019)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="V -> G (in Ref. 1; AAG31018/AAG31019)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="E -> G (in Ref. 2; BAB55264)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="S -> Y (in Ref. 1; AAG31019)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="P -> L (in Ref. 2; BAB15256)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="L -> M (in Ref. 2; BAB55291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 83394 MW; EA1909828FAE685E CRC64;
MAVRALKLLT TLLAVVAAAS QAEVESEAGW GMVTPDLLFA EGTAAYARGD WPGVVLSMER
ALRSRAALRA LRLRCRTQCA ADFPWELDPD WSPSPAQASG AAALRDLSFF GGLLRRAACL
RRCLGPPAAH SLSEEMELEF RKRSPYNYLQ VAYFKINKLE KAVAAAHTFF VGNPEHMEMQ
QNLDYYQTMS GVKEADFKDL ETQPHMQEFR LGVRLYSEEQ PQEAVPHLEA ALQEYFVAYE
ECRALCEGPY DYDGYNYLEY NADLFQAITD HYIQVLNCKQ NCVTELASHP SREKPFEDFL
PSHYNYLQFA YYNIGNYTQA VECAKTYLLF FPNDEVMNQN LAYYAAMLGE EHTRSIGPRE
SAKEYRQRSL LEKELLFFAY DVFGIPFVDP DSWTPEEVIP KRLQEKQKSE RETAVRISQE
IGNLMKEIET LVEEKTKESL DVSRLTREGG PLLYEGISLT MNSKLLNGSQ RVVMDGVISD
HECQELQRLT NVAATSGDGY RGQTSPHTPN EKFYGVTVFK ALKLGQEGKV PLQSAHLYYN
VTEKVRRIME SYFRLDTPLY FSYSHLVCRT AIEEVQAERK DDSHPVHVDN CILNAETLVC
VKEPPAYTFR DYSAILYLNG DFDGGNFYFT ELDAKTVTAE VQPQCGRAVG FSSGTENPHG
VKAVTRGQRC AIALWFTLDP RHSERDRVQA DDLVKMLFSP EEMDLSQEQP LDAQQGPPEP
AQESLSGSES KPKDEL
