SMOC2_HUMAN
ID SMOC2_HUMAN Reviewed; 446 AA.
AC Q9H3U7; B3KPS7; Q4G169; Q5TAT7; Q5TAT8; Q86VV9; Q96SF3; Q9H1L3; Q9H1L4;
AC Q9H3U0; Q9H4F7; Q9HCV2;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=SPARC-related modular calcium-binding protein 2;
DE AltName: Full=Secreted modular calcium-binding protein 2;
DE Short=SMOC-2;
DE AltName: Full=Smooth muscle-associated protein 2;
DE Short=SMAP-2;
DE Flags: Precursor;
GN Name=SMOC2; Synonyms=SMAP2; ORFNames=MSTP117;
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 TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=12031507; DOI=10.1016/s0167-4781(02)00345-7;
RA Nishimoto S., Hamajima Y., Toda Y., Toyoda H., Kitamura K., Komurasaki T.;
RT "Identification of a novel smooth muscle associated protein, smap2,
RT upregulated during neointima formation in a rat carotid endarterectomy
RT model.";
RL Biochim. Biophys. Acta 1576:225-230(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-446 (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu Y.Q., Liu B., Wang X.Y., Sheng H., Qin B.M., Zhang Q., Zheng W.Y.,
RA Hui R.T.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-446.
RC TISSUE=Fetal brain;
RX PubMed=12741954; DOI=10.1042/bj20030532;
RA Vannahme C., Goesling S., Paulsson M., Maurer P., Hartmann U.;
RT "Characterization of SMOC-2, a modular extracellular calcium-binding
RT protein.";
RL Biochem. J. 373:805-814(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16774925; DOI=10.1074/jbc.m513463200;
RA Rocnik E.F., Liu P., Sato K., Walsh K., Vaziri C.;
RT "The novel SPARC family member SMOC-2 potentiates angiogenic growth factor
RT activity.";
RL J. Biol. Chem. 281:22855-22864(2006).
RN [10]
RP INVOLVEMENT IN DTDP1.
RX PubMed=22152679; DOI=10.1016/j.ajhg.2011.11.002;
RA Bloch-Zupan A., Jamet X., Etard C., Laugel V., Muller J., Geoffroy V.,
RA Strauss J.P., Pelletier V., Marion V., Poch O., Strahle U., Stoetzel C.,
RA Dollfus H.;
RT "Homozygosity mapping and candidate prioritization identify mutations,
RT missed by whole-exome sequencing, in SMOC2, causing major dental
RT developmental defects.";
RL Am. J. Hum. Genet. 89:773-781(2011).
CC -!- FUNCTION: Promotes matrix assembly and cell adhesiveness (By
CC similarity). Can stimulate endothelial cell proliferation, migration,
CC as well as angiogenesis. {ECO:0000250, ECO:0000269|PubMed:16774925}.
CC -!- SUBUNIT: Binds various proteins from the extracellular matrix.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9H3U7; Q6L8H4: KRTAP5-1; NbExp=3; IntAct=EBI-12767060, EBI-12074540;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Smap2;
CC IsoId=Q9H3U7-1; Sequence=Displayed;
CC Name=2; Synonyms=Smap2b;
CC IsoId=Q9H3U7-2; Sequence=VSP_008722;
CC -!- DISEASE: Dentin dysplasia 1 (DTDP1) [MIM:125400]: A dental defect in
CC which both primary and secondary dentitions are affected. The clinical
CC crowns of both permanent and deciduous teeth are of normal shape, form
CC and color in most cases, although they may be slightly opalescent and
CC blue or brown. Teeth may be very mobile and exfoliate spontaneously
CC because of inadequate root formation. On radiographs, the roots are
CC short and may be more pointed than normal. Pulp chambers are usually
CC absent except for a chevron-shaped remnant in the crown. Root canals
CC are usually absent. {ECO:0000269|PubMed:22152679}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13639.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AB014730; BAB20267.1; -; mRNA.
DR EMBL; AB014737; BAB20274.1; -; mRNA.
DR EMBL; AK056700; BAG51789.1; -; mRNA.
DR EMBL; AL832303; CAI46175.1; -; mRNA.
DR EMBL; AL109940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47462.1; -; Genomic_DNA.
DR EMBL; BC028420; AAH28420.1; -; mRNA.
DR EMBL; BC047583; AAH47583.1; -; mRNA.
DR EMBL; AF173892; AAQ13639.1; ALT_INIT; mRNA.
DR EMBL; AJ249902; CAC10353.1; -; mRNA.
DR CCDS; CCDS5307.1; -. [Q9H3U7-2]
DR CCDS; CCDS55076.1; -. [Q9H3U7-1]
DR RefSeq; NP_001159884.1; NM_001166412.1. [Q9H3U7-1]
DR RefSeq; NP_071421.1; NM_022138.2. [Q9H3U7-2]
DR AlphaFoldDB; Q9H3U7; -.
DR BioGRID; 122056; 6.
DR IntAct; Q9H3U7; 1.
DR STRING; 9606.ENSP00000346537; -.
DR GlyGen; Q9H3U7; 2 sites.
DR iPTMnet; Q9H3U7; -.
DR PhosphoSitePlus; Q9H3U7; -.
DR BioMuta; SMOC2; -.
DR DMDM; 38258648; -.
DR jPOST; Q9H3U7; -.
DR MassIVE; Q9H3U7; -.
DR MaxQB; Q9H3U7; -.
DR PaxDb; Q9H3U7; -.
DR PeptideAtlas; Q9H3U7; -.
DR PRIDE; Q9H3U7; -.
DR ProteomicsDB; 80763; -. [Q9H3U7-1]
DR ProteomicsDB; 80764; -. [Q9H3U7-2]
DR Antibodypedia; 33562; 138 antibodies from 24 providers.
DR DNASU; 64094; -.
DR Ensembl; ENST00000354536.9; ENSP00000346537.5; ENSG00000112562.20. [Q9H3U7-2]
DR Ensembl; ENST00000356284.7; ENSP00000348630.3; ENSG00000112562.20. [Q9H3U7-1]
DR GeneID; 64094; -.
DR KEGG; hsa:64094; -.
DR MANE-Select; ENST00000356284.7; ENSP00000348630.3; NM_001166412.2; NP_001159884.1.
DR UCSC; uc003qwr.2; human. [Q9H3U7-1]
DR CTD; 64094; -.
DR DisGeNET; 64094; -.
DR GeneCards; SMOC2; -.
DR HGNC; HGNC:20323; SMOC2.
DR HPA; ENSG00000112562; Low tissue specificity.
DR MalaCards; SMOC2; -.
DR MIM; 125400; phenotype.
DR MIM; 607223; gene.
DR neXtProt; NX_Q9H3U7; -.
DR OpenTargets; ENSG00000112562; -.
DR Orphanet; 314721; Atypical dentin dysplasia due to SMOC2 deficiency.
DR PharmGKB; PA134934590; -.
DR VEuPathDB; HostDB:ENSG00000112562; -.
DR eggNOG; KOG4578; Eukaryota.
DR GeneTree; ENSGT00390000018436; -.
DR HOGENOM; CLU_023483_0_0_1; -.
DR InParanoid; Q9H3U7; -.
DR OMA; AYRGNCR; -.
DR OrthoDB; 1057719at2759; -.
DR PhylomeDB; Q9H3U7; -.
DR TreeFam; TF320666; -.
DR PathwayCommons; Q9H3U7; -.
DR SignaLink; Q9H3U7; -.
DR BioGRID-ORCS; 64094; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; SMOC2; human.
DR GeneWiki; SMOC2; -.
DR GenomeRNAi; 64094; -.
DR Pharos; Q9H3U7; Tbio.
DR PRO; PR:Q9H3U7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H3U7; protein.
DR Bgee; ENSG00000112562; Expressed in descending thoracic aorta and 163 other tissues.
DR ExpressionAtlas; Q9H3U7; baseline and differential.
DR Genevisible; Q9H3U7; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISA:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IGI:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; IDA:UniProtKB.
DR CDD; cd16241; EFh_SPARC_SMOC2; 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; IPR002048; EF_hand_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR037640; SMOC2_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; PS50222; EF_HAND_2; 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; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..446
FT /note="SPARC-related modular calcium-binding protein 2"
FT /id="PRO_0000020318"
FT DOMAIN 34..86
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 87..153
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 213..281
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 347..382
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 384..419
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 147..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 44..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 53..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 90..113
FT /evidence="ECO:0000250"
FT DISULFID 124..131
FT /evidence="ECO:0000250"
FT DISULFID 133..153
FT /evidence="ECO:0000250"
FT DISULFID 216..240
FT /evidence="ECO:0000250"
FT DISULFID 251..258
FT /evidence="ECO:0000250"
FT DISULFID 260..281
FT /evidence="ECO:0000250"
FT VAR_SEQ 170
FT /note="T -> TVSLQIFSVLNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12031507,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_008722"
FT CONFLICT 169..170
FT /note="KT -> TR (in Ref. 8; CAC10353)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="S -> P (in Ref. 1; BAB20267)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="A -> V (in Ref. 6; AAH47583)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="N -> Y (in Ref. 8; CAC10353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49674 MW; CF0D92A71C9E1006 CRC64;
MLLPQLCWLP LLAGLLPPVP AQKFSALTFL RVDQDKDKDC SLDCAGSPQK PLCASDGRTF
LSRCEFQRAK CKDPQLEIAY RGNCKDVSRC VAERKYTQEQ ARKEFQQVFI PECNDDGTYS
QVQCHSYTGY CWCVTPNGRP ISGTAVAHKT PRCPGSVNEK LPQREGTGKT DDAAAPALET
QPQGDEEDIA SRYPTLWTEQ VKSRQNKTNK NSVSSCDQEH QSALEEAKQP KNDNVVIPEC
AHGGLYKPVQ CHPSTGYCWC VLVDTGRPIP GTSTRYEQPK CDNTARAHPA KARDLYKGRQ
LQGCPGAKKH EFLTSVLDAL STDMVHAASD PSSSSGRLSE PDPSHTLEER VVHWYFKLLD
KNSSGDIGKK EIKPFKRFLR KKSKPKKCVK KFVEYCDVNN DKSISVQELM GCLGVAKEDG
KADTKKRHTP RGHAESTSNR QPRKQG
