BOC_HUMAN
ID BOC_HUMAN Reviewed; 1114 AA.
AC Q9BWV1; A6NJ30; B2RMS8; D3DN70; Q6UXJ5; Q8N2P7; Q8NF26;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Brother of CDO;
DE Short=Protein BOC;
DE Flags: Precursor;
GN Name=BOC; ORFNames=UNQ604/PRO1190;
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), INTERACTION WITH CDON,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11782431; DOI=10.1093/emboj/21.1.114;
RA Kang J.-S., Mulieri P.J., Hu Y., Taliana L., Krauss R.S.;
RT "BOC, an Ig superfamily member, associates with CDO to positively regulate
RT myogenic differentiation.";
RL EMBO J. 21:114-124(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-1114 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-1114 (ISOFORM 2).
RC TISSUE=Embryo, and Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PROTEIN SEQUENCE OF 31-45.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH CDON; CDH2; CDH15 AND CTNNB1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12634428; DOI=10.1073/pnas.0736565100;
RA Kang J.-S., Feinleib J.L., Knox S., Ketteringham M.A., Krauss R.S.;
RT "Promyogenic members of the Ig and cadherin families associate to
RT positively regulate differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3989-3994(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 710-817 IN COMPLEXES WITH DHH AND
RP IHH, AND INTERACTION WITH SHH; DHH AND IHH.
RX PubMed=20519495; DOI=10.1074/jbc.m110.131680;
RA Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.;
RT "All mammalian Hedgehog proteins interact with cell adhesion molecule,
RT down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved
RT manner.";
RL J. Biol. Chem. 285:24584-24590(2010).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] MET-713.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of a cell-surface receptor complex that mediates
CC cell-cell interactions between muscle precursor cells. Promotes
CC differentiation of myogenic cells.
CC -!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1, cadherins and
CC CTNNB1. Interacts with NTN3 (By similarity). Interacts with SHH, DHH
CC and IHH. Interacts with CDH2 and CTNNB1. Interacts with CDH15 only
CC during the early stages of myoblast differentiation. {ECO:0000250,
CC ECO:0000269|PubMed:11782431, ECO:0000269|PubMed:12634428,
CC ECO:0000269|PubMed:20519495}.
CC -!- INTERACTION:
CC Q9BWV1; O43323: DHH; NbExp=2; IntAct=EBI-718555, EBI-11667804;
CC Q9BWV1; Q14623: IHH; NbExp=2; IntAct=EBI-718555, EBI-3918622;
CC Q9BWV1; O35158: Cdon; Xeno; NbExp=2; IntAct=EBI-718555, EBI-7016767;
CC Q9BWV1; Q01721: Gas1; Xeno; NbExp=2; IntAct=EBI-718555, EBI-15729104;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12634428};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12634428}.
CC Note=Enriched at sites of cell-cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BWV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWV1-3; Sequence=VSP_034684;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart, thymus, kidney
CC and small intestine. Detected at lower levels in brain, placenta, lung
CC and colon mucosa. {ECO:0000269|PubMed:11782431}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11782431}.
CC -!- MISCELLANEOUS: The C-terminal cytoplasmic domain is not required for
CC the stimulation of myogenesis.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03436.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAC11057.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY027658; AAK14795.1; -; mRNA.
DR EMBL; AY358328; AAQ88694.1; -; mRNA.
DR EMBL; AK074556; BAC11057.1; ALT_INIT; mRNA.
DR EMBL; AK090455; BAC03436.1; ALT_SEQ; mRNA.
DR EMBL; AC026329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79643.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79644.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79646.1; -; Genomic_DNA.
DR EMBL; BC136390; AAI36391.1; -; mRNA.
DR CCDS; CCDS2971.1; -. [Q9BWV1-1]
DR CCDS; CCDS77788.1; -. [Q9BWV1-3]
DR RefSeq; NP_001288790.1; NM_001301861.1. [Q9BWV1-3]
DR RefSeq; NP_150279.1; NM_033254.3. [Q9BWV1-1]
DR RefSeq; XP_005247948.1; XM_005247891.2.
DR RefSeq; XP_005247949.1; XM_005247892.2.
DR RefSeq; XP_011511607.1; XM_011513305.2. [Q9BWV1-1]
DR RefSeq; XP_016862940.1; XM_017007451.1.
DR PDB; 3N1G; X-ray; 1.90 A; C/D=710-817.
DR PDB; 3N1M; X-ray; 1.69 A; C=710-817.
DR PDB; 3N1P; X-ray; 2.70 A; C=710-817.
DR PDBsum; 3N1G; -.
DR PDBsum; 3N1M; -.
DR PDBsum; 3N1P; -.
DR AlphaFoldDB; Q9BWV1; -.
DR SMR; Q9BWV1; -.
DR BioGRID; 124859; 25.
DR IntAct; Q9BWV1; 14.
DR STRING; 9606.ENSP00000418663; -.
DR GlyGen; Q9BWV1; 9 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWV1; -.
DR PhosphoSitePlus; Q9BWV1; -.
DR BioMuta; BOC; -.
DR DMDM; 74761309; -.
DR MassIVE; Q9BWV1; -.
DR PaxDb; Q9BWV1; -.
DR PeptideAtlas; Q9BWV1; -.
DR PRIDE; Q9BWV1; -.
DR ProteomicsDB; 79319; -. [Q9BWV1-1]
DR ProteomicsDB; 79321; -. [Q9BWV1-3]
DR Antibodypedia; 32560; 170 antibodies from 32 providers.
DR DNASU; 91653; -.
DR Ensembl; ENST00000273395.8; ENSP00000273395.4; ENSG00000144857.15. [Q9BWV1-3]
DR Ensembl; ENST00000355385.7; ENSP00000347546.3; ENSG00000144857.15. [Q9BWV1-1]
DR Ensembl; ENST00000495514.5; ENSP00000418663.1; ENSG00000144857.15. [Q9BWV1-1]
DR Ensembl; ENST00000682979.1; ENSP00000507783.1; ENSG00000144857.15. [Q9BWV1-3]
DR GeneID; 91653; -.
DR KEGG; hsa:91653; -.
DR MANE-Select; ENST00000682979.1; ENSP00000507783.1; NM_001378074.1; NP_001365003.1. [Q9BWV1-3]
DR UCSC; uc003dzx.4; human. [Q9BWV1-1]
DR CTD; 91653; -.
DR DisGeNET; 91653; -.
DR GeneCards; BOC; -.
DR HGNC; HGNC:17173; BOC.
DR HPA; ENSG00000144857; Low tissue specificity.
DR MIM; 608708; gene.
DR neXtProt; NX_Q9BWV1; -.
DR OpenTargets; ENSG00000144857; -.
DR PharmGKB; PA143485316; -.
DR VEuPathDB; HostDB:ENSG00000144857; -.
DR eggNOG; ENOG502QUNT; Eukaryota.
DR GeneTree; ENSGT00940000158810; -.
DR HOGENOM; CLU_008503_0_0_1; -.
DR InParanoid; Q9BWV1; -.
DR OMA; VVWLRNA; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; Q9BWV1; -.
DR TreeFam; TF332268; -.
DR PathwayCommons; Q9BWV1; -.
DR Reactome; R-HSA-525793; Myogenesis. [Q9BWV1-1]
DR Reactome; R-HSA-5632681; Ligand-receptor interactions.
DR Reactome; R-HSA-5635838; Activation of SMO.
DR SignaLink; Q9BWV1; -.
DR SIGNOR; Q9BWV1; -.
DR BioGRID-ORCS; 91653; 12 hits in 1062 CRISPR screens.
DR ChiTaRS; BOC; human.
DR EvolutionaryTrace; Q9BWV1; -.
DR GeneWiki; BOC_(gene); -.
DR GenomeRNAi; 91653; -.
DR Pharos; Q9BWV1; Tbio.
DR PRO; PR:Q9BWV1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BWV1; protein.
DR Bgee; ENSG00000144857; Expressed in tendon of biceps brachii and 175 other tissues.
DR ExpressionAtlas; Q9BWV1; baseline and differential.
DR Genevisible; Q9BWV1; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:HGNC.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR032982; BOC.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR44170:SF3; PTHR44170:SF3; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 31..1114
FT /note="Brother of CDO"
FT /id="PRO_0000234052"
FT TOPO_DOM 31..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..1114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 129..213
FT /note="Ig-like C2-type 2"
FT DOMAIN 235..315
FT /note="Ig-like C2-type 3"
FT DOMAIN 323..409
FT /note="Ig-like C2-type 4"
FT DOMAIN 474..571
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 608..703
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 712..812
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 422..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 252..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 344..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 514
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_034684"
FT VARIANT 713
FT /note="V -> M (in a breast cancer sample; somatic mutation;
FT dbSNP:rs367589886)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035503"
FT VARIANT 883
FT /note="K -> N (in dbSNP:rs35536878)"
FT /id="VAR_033600"
FT VARIANT 915
FT /note="Q -> H (in dbSNP:rs3814405)"
FT /id="VAR_033601"
FT CONFLICT 461
FT /note="Q -> K (in Ref. 2; AAQ88694)"
FT /evidence="ECO:0000305"
FT STRAND 717..725
FT /evidence="ECO:0007829|PDB:3N1M"
FT STRAND 728..734
FT /evidence="ECO:0007829|PDB:3N1M"
FT HELIX 737..740
FT /evidence="ECO:0007829|PDB:3N1M"
FT STRAND 746..754
FT /evidence="ECO:0007829|PDB:3N1M"
FT HELIX 760..762
FT /evidence="ECO:0007829|PDB:3N1M"
FT STRAND 764..769
FT /evidence="ECO:0007829|PDB:3N1M"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:3N1M"
FT STRAND 785..794
FT /evidence="ECO:0007829|PDB:3N1M"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:3N1M"
SQ SEQUENCE 1114 AA; 121059 MW; BDA9021D39CFE3BC CRC64;
MLRGTMTAWR GMRPEVTLAC LLLATAGCFA DLNEVPQVTV QPASTVQKPG GTVILGCVVE
PPRMNVTWRL NGKELNGSDD ALGVLITHGT LVITALNNHT VGRYQCVARM PAGAVASVPA
TVTLANLQDF KLDVQHVIEV DEGNTAVIAC HLPESHPKAQ VRYSVKQEWL EASRGNYLIM
PSGNLQIVNA SQEDEGMYKC AAYNPVTQEV KTSGSSDRLR VRRSTAEAAR IIYPPEAQTI
IVTKGQSLIL ECVASGIPPP RVTWAKDGSS VTGYNKTRFL LSNLLIDTTS EEDSGTYRCM
ADNGVGQPGA AVILYNVQVF EPPEVTMELS QLVIPWGQSA KLTCEVRGNP PPSVLWLRNA
VPLISSQRLR LSRRALRVLS MGPEDEGVYQ CMAENEVGSA HAVVQLRTSR PSITPRLWQD
AELATGTPPV SPSKLGNPEQ MLRGQPALPR PPTSVGPASP QCPGEKGQGA PAEAPIILSS
PRTSKTDSYE LVWRPRHEGS GRAPILYYVV KHRKVTNSSD DWTISGIPAN QHRLTLTRLD
PGSLYEVEMA AYNCAGEGQT AMVTFRTGRR PKPEIMASKE QQIQRDDPGA SPQSSSQPDH
GRLSPPEAPD RPTISTASET SVYVTWIPRG NGGFPIQSFR VEYKKLKKVG DWILATSAIP
PSRLSVEITG LEKGTSYKFR VRALNMLGES EPSAPSRPYV VSGYSGRVYE RPVAGPYITF
TDAVNETTIM LKWMYIPASN NNTPIHGFYI YYRPTDSDND SDYKKDMVEG DKYWHSISHL
QPETSYDIKM QCFNEGGESE FSNVMICETK ARKSSGQPGR LPPPTLAPPQ PPLPETIERP
VGTGAMVARS SDLPYLIVGV VLGSIVLIIV TFIPFCLWRA WSKQKHTTDL GFPRSALPPS
CPYTMVPLGG LPGHQASGQP YLSGISGRAC ANGIHMNRGC PSAAVGYPGM KPQQHCPGEL
QQQSDTSSLL RQTHLGNGYD PQSHQITRGP KSSPDEGSFL YTLPDDSTHQ LLQPHHDCCQ
RQEQPAAVGQ SGVRRAPDSP VLEAVWDPPF HSGPPCCLGL VPVEEVDSPD SCQVSGGDWC
PQHPVGAYVG QEPGMQLSPG PLVRVSFETP PLTI
