SMOC1_HUMAN
ID SMOC1_HUMAN Reviewed; 434 AA.
AC Q9H4F8; A8K1S3; B2R7P5; Q96F78;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=SPARC-related modular calcium-binding protein 1;
DE AltName: Full=Secreted modular calcium-binding protein 1;
DE Short=SMOC-1;
DE Flags: Precursor;
GN Name=SMOC1;
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] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RC TISSUE=Fetal brain;
RX PubMed=12130637; DOI=10.1074/jbc.m203830200;
RA Vannahme C., Smyth N., Miosge N., Goesling S., Frie C., Paulsson M.,
RA Maurer P., Hartmann U.;
RT "Characterization of SMOC-1, a novel modular calcium-binding protein in
RT basement membranes.";
RL J. Biol. Chem. 277:37977-37986(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate nucleus;
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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Lung;
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 [6]
RP FUNCTION AS REGULATOR OF OSTEOBLAST DIFFERENTIATION, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20359165; DOI=10.1021/pr901110q;
RA Choi Y.A., Lim J., Kim K.M., Acharya B., Cho J.Y., Bae Y.C., Shin H.I.,
RA Kim S.Y., Park E.K.;
RT "Secretome analysis of human BMSCs and identification of SMOC1 as an
RT important ECM protein in osteoblast differentiation.";
RL J. Proteome Res. 9:2946-2956(2010).
RN [7]
RP FUNCTION, AND INVOLVEMENT IN OAS.
RX PubMed=21194678; DOI=10.1016/j.ajhg.2010.11.012;
RA Okada I., Hamanoue H., Terada K., Tohma T., Megarbane A., Chouery E.,
RA Abou-Ghoch J., Jalkh N., Cogulu O., Ozkinay F., Horie K., Takeda J.,
RA Furuichi T., Ikegawa S., Nishiyama K., Miyatake S., Nishimura A.,
RA Mizuguchi T., Niikawa N., Hirahara F., Kaname T., Yoshiura K.,
RA Tsurusaki Y., Doi H., Miyake N., Furukawa T., Matsumoto N., Saitsu H.;
RT "SMOC1 is essential for ocular and limb development in humans and mice.";
RL Am. J. Hum. Genet. 88:30-41(2011).
RN [8]
RP FUNCTION, AND INVOLVEMENT IN OAS.
RX PubMed=21194680; DOI=10.1016/j.ajhg.2010.12.002;
RA Abouzeid H., Boisset G., Favez T., Youssef M., Marzouk I., Shakankiry N.,
RA Bayoumi N., Descombes P., Agosti C., Munier F.L., Schorderet D.F.;
RT "Mutations in the SPARC-related modular calcium-binding protein 1 gene,
RT SMOC1, cause waardenburg anophthalmia syndrome.";
RL Am. J. Hum. Genet. 88:92-98(2011).
RN [9]
RP VARIANTS OAS CYS-278 AND ASN-283.
RX PubMed=21750680; DOI=10.1371/journal.pgen.1002114;
RA Rainger J., van Beusekom E., Ramsay J.K., McKie L., Al-Gazali L.,
RA Pallotta R., Saponari A., Branney P., Fisher M., Morrison H., Bicknell L.,
RA Gautier P., Perry P., Sokhi K., Sexton D., Bardakjian T.M., Schneider A.S.,
RA Elcioglu N., Ozkinay F., Koenig R., Megarbane A., Semerci C.N., Khan A.,
RA Zafar S., Hennekam R., Sousa S.B., Ramos L., Garavelli L., Furga A.S.,
RA Wischmeijer A., Jackson I.J., Gillessen-Kaesbach G., Brunner H.G.,
RA Wieczorek D., van Bokhoven H., Fitzpatrick D.R.;
RT "Loss of the BMP antagonist, SMOC-1, causes Ophthalmo-acromelic
RT (Waardenburg Anophthalmia) syndrome in humans and mice.";
RL PLoS Genet. 7:E1002114-E1002114(2011).
RN [10]
RP VARIANT OAS HIS-286.
RX PubMed=23646827; DOI=10.1111/cge.12184;
RA Aldahmesh M.A., Khan A.O., Hijazi H., Alkuraya F.S.;
RT "Mutations in ALDH1A3 cause Microphthalmia.";
RL Clin. Genet. 84:128-131(2013).
CC -!- FUNCTION: Plays essential roles in both eye and limb development.
CC Probable regulator of osteoblast differentiation.
CC {ECO:0000269|PubMed:20359165, ECO:0000269|PubMed:21194678,
CC ECO:0000269|PubMed:21194680}.
CC -!- INTERACTION:
CC Q9H4F8; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2801103, EBI-10171774;
CC Q9H4F8; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-2801103, EBI-945833;
CC Q9H4F8; P15884: TCF4; NbExp=3; IntAct=EBI-2801103, EBI-533224;
CC Q9H4F8; P09022: Hoxa1; Xeno; NbExp=2; IntAct=EBI-2801103, EBI-3957603;
CC Q9H4F8-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12162539, EBI-3867333;
CC Q9H4F8-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12162539, EBI-11959885;
CC Q9H4F8-2; Q92570: NR4A3; NbExp=3; IntAct=EBI-12162539, EBI-13644623;
CC Q9H4F8-2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-12162539, EBI-11957216;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:12130637,
CC ECO:0000269|PubMed:20359165}. Note=In or around the basement membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4F8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4F8-2; Sequence=VSP_008720;
CC -!- TISSUE SPECIFICITY: Widely expressed in many tissues with a strongest
CC signal in ovary. No expression in spleen.
CC {ECO:0000269|PubMed:12130637}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12130637}.
CC -!- DISEASE: Ophthalmoacromelic syndrome (OAS) [MIM:206920]: A rare
CC disorder presenting with ocular anomalies, ranging from mild
CC microphthalmia to true anophthalmia, and limb anomalies. Limb
CC malformations include fused 4th and 5th metacarpals and short 5th
CC finger in hands, and oligodactyly in foot (four toes). Most patients
CC have bilateral anophthalmia/ microphthalmia, but unilateral abnormality
CC is also noted. Other malformations are rare, but venous or vertebral
CC anomaly was recognized each in single cases.
CC {ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21194680,
CC ECO:0000269|PubMed:21750680, ECO:0000269|PubMed:23646827}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AJ249900; CAC10352.1; -; mRNA.
DR EMBL; AK289988; BAF82677.1; -; mRNA.
DR EMBL; AK313063; BAG35892.1; -; mRNA.
DR EMBL; AL135747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81013.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81014.1; -; Genomic_DNA.
DR EMBL; BC008608; AAH08608.1; -; mRNA.
DR EMBL; BC011548; AAH11548.1; -; mRNA.
DR CCDS; CCDS32110.1; -. [Q9H4F8-2]
DR CCDS; CCDS9798.1; -. [Q9H4F8-1]
DR RefSeq; NP_001030024.1; NM_001034852.2. [Q9H4F8-2]
DR RefSeq; NP_071420.1; NM_022137.5. [Q9H4F8-1]
DR AlphaFoldDB; Q9H4F8; -.
DR BioGRID; 122055; 57.
DR IntAct; Q9H4F8; 31.
DR MINT; Q9H4F8; -.
DR STRING; 9606.ENSP00000355110; -.
DR GlyGen; Q9H4F8; 5 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9H4F8; -.
DR PhosphoSitePlus; Q9H4F8; -.
DR BioMuta; SMOC1; -.
DR DMDM; 38258649; -.
DR EPD; Q9H4F8; -.
DR jPOST; Q9H4F8; -.
DR MassIVE; Q9H4F8; -.
DR MaxQB; Q9H4F8; -.
DR PaxDb; Q9H4F8; -.
DR PeptideAtlas; Q9H4F8; -.
DR PRIDE; Q9H4F8; -.
DR ProteomicsDB; 80829; -. [Q9H4F8-1]
DR ProteomicsDB; 80830; -. [Q9H4F8-2]
DR Antibodypedia; 125; 129 antibodies from 20 providers.
DR DNASU; 64093; -.
DR Ensembl; ENST00000361956.8; ENSP00000355110.4; ENSG00000198732.11. [Q9H4F8-2]
DR Ensembl; ENST00000381280.4; ENSP00000370680.4; ENSG00000198732.11. [Q9H4F8-1]
DR GeneID; 64093; -.
DR KEGG; hsa:64093; -.
DR MANE-Select; ENST00000361956.8; ENSP00000355110.4; NM_001034852.3; NP_001030024.1. [Q9H4F8-2]
DR UCSC; uc001xls.3; human. [Q9H4F8-1]
DR CTD; 64093; -.
DR DisGeNET; 64093; -.
DR GeneCards; SMOC1; -.
DR HGNC; HGNC:20318; SMOC1.
DR HPA; ENSG00000198732; Tissue enhanced (brain, liver).
DR MalaCards; SMOC1; -.
DR MIM; 206920; phenotype.
DR MIM; 608488; gene.
DR neXtProt; NX_Q9H4F8; -.
DR OpenTargets; ENSG00000198732; -.
DR Orphanet; 1106; Microphthalmia with limb anomalies.
DR PharmGKB; PA134942329; -.
DR VEuPathDB; HostDB:ENSG00000198732; -.
DR eggNOG; KOG4578; Eukaryota.
DR GeneTree; ENSGT00390000018436; -.
DR HOGENOM; CLU_023483_0_0_1; -.
DR InParanoid; Q9H4F8; -.
DR OMA; MPNCESD; -.
DR OrthoDB; 1057719at2759; -.
DR PhylomeDB; Q9H4F8; -.
DR TreeFam; TF320666; -.
DR PathwayCommons; Q9H4F8; -.
DR SignaLink; Q9H4F8; -.
DR SIGNOR; Q9H4F8; -.
DR BioGRID-ORCS; 64093; 6 hits in 1071 CRISPR screens.
DR ChiTaRS; SMOC1; human.
DR GenomeRNAi; 64093; -.
DR Pharos; Q9H4F8; Tbio.
DR PRO; PR:Q9H4F8; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H4F8; protein.
DR Bgee; ENSG00000198732; Expressed in ganglionic eminence and 153 other tissues.
DR ExpressionAtlas; Q9H4F8; baseline and differential.
DR Genevisible; Q9H4F8; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:UniProtKB.
DR CDD; cd16240; EFh_SPARC_SMOC1; 1.
DR CDD; cd00191; TY; 2.
DR Gene3D; 4.10.800.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR037639; SMOC1_EC.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF57610; SSF57610; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Developmental protein;
KW Differentiation; Disease variant; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Metal-binding; Microphthalmia; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..434
FT /note="SPARC-related modular calcium-binding protein 1"
FT /id="PRO_0000020316"
FT DOMAIN 37..89
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 92..158
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 224..292
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 359..394
FT /note="EF-hand 1"
FT DOMAIN 396..431
FT /note="EF-hand 2"
FT REGION 149..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 47..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 56..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 95..118
FT /evidence="ECO:0000250"
FT DISULFID 129..136
FT /evidence="ECO:0000250"
FT DISULFID 138..158
FT /evidence="ECO:0000250"
FT DISULFID 227..251
FT /evidence="ECO:0000250"
FT DISULFID 262..269
FT /evidence="ECO:0000250"
FT DISULFID 271..292
FT /evidence="ECO:0000250"
FT VAR_SEQ 430
FT /note="E -> EV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008720"
FT VARIANT 82
FT /note="V -> M (in dbSNP:rs10150925)"
FT /id="VAR_034498"
FT VARIANT 278
FT /note="R -> C (in OAS; dbSNP:rs776638586)"
FT /evidence="ECO:0000269|PubMed:21750680"
FT /id="VAR_069326"
FT VARIANT 283
FT /note="T -> N (in OAS)"
FT /evidence="ECO:0000269|PubMed:21750680"
FT /id="VAR_069327"
FT VARIANT 286
FT /note="R -> H (in OAS; dbSNP:rs1365818420)"
FT /evidence="ECO:0000269|PubMed:23646827"
FT /id="VAR_069328"
SQ SEQUENCE 434 AA; 48163 MW; 2CB639212BA42478 CRC64;
MLPARCARLL TPHLLLVLVQ LSPARGHRTT GPRFLISDRD PQCNLHCSRT QPKPICASDG
RSYESMCEYQ RAKCRDPTLG VVHRGRCKDA GQSKCRLERA QALEQAKKPQ EAVFVPECGE
DGSFTQVQCH TYTGYCWCVT PDGKPISGSS VQNKTPVCSG SVTDKPLSQG NSGRKDDGSK
PTPTMETQPV FDGDEITAPT LWIKHLVIKD SKLNNTNIRN SEKVYSCDQE RQSALEEAQQ
NPREGIVIPE CAPGGLYKPV QCHQSTGYCW CVLVDTGRPL PGTSTRYVMP SCESDARAKT
TEADDPFKDR ELPGCPEGKK MEFITSLLDA LTTDMVQAIN SAAPTGGGRF SEPDPSHTLE
ERVVHWYFSQ LDSNSSNDIN KREMKPFKRY VKKKAKPKKC ARRFTDYCDL NKDKVISLPE
LKGCLGVSKE GRLV
