NCAM1_HUMAN
ID NCAM1_HUMAN Reviewed; 858 AA.
AC P13591; A8K8T8; P13592; P13593; Q05C58; Q15829; Q16180; Q16209; Q59FL7;
AC Q86X47; Q96CJ3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Neural cell adhesion molecule 1;
DE Short=N-CAM-1;
DE Short=NCAM-1;
DE AltName: CD_antigen=CD56;
DE Flags: Precursor;
GN Name=NCAM1; Synonyms=NCAM;
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 3).
RC TISSUE=Skeletal muscle;
RX PubMed=3253057; DOI=10.1242/dev.104.1.165;
RA Barton C.H., Dickson G., Gower H.J., Rowett L.H., Putt W., Elsom V.,
RA Moore S.E., Goridis C., Walsh F.S.;
RT "Complete sequence and in vitro expression of a tissue-specific
RT phosphatidylinositol-linked N-CAM isoform from skeletal muscle.";
RL Development 104:165-173(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1710251;
RA Lanier L.L., Chang C., Azuma M., Ruitenberg J.J., Hemperly J.J.,
RA Phillips J.H.;
RT "Molecular and functional analysis of human natural killer cell-associated
RT neural cell adhesion molecule (N-CAM/CD56).";
RL J. Immunol. 146:4421-4426(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8075973; DOI=10.1016/0169-5002(94)90660-2;
RA Saito S., Tanio Y., Tachibana I., Hayashi S., Kishimoto T., Kawase I.;
RT "Complementary DNA sequence encoding the major neural cell adhesion
RT molecule isoform in a human small cell lung cancer cell line.";
RL Lung Cancer 10:307-318(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT
RP ASP-679.
RC TISSUE=Brain, Kidney, and Ovary;
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 [MRNA] OF 347-369.
RX PubMed=1339414; DOI=10.1002/ijc.2910500124;
RA van Duijnhoven H.L., Helfrich W., de Leij L., Roebroek A.J.,
RA van de Ven W.J., Healey K., Culverwell A., Rossell R.J., Kemshead J.T.,
RA Patel K.;
RT "Splicing of the VASE exon of neural cell adhesion molecule (NCAM) in human
RT small-cell lung carcinoma (SCLC).";
RL Int. J. Cancer 50:118-123(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-858 (ISOFORMS 1/2 AND 3).
RC TISSUE=Skeletal muscle;
RX PubMed=2887295; DOI=10.1016/0092-8674(87)90178-4;
RA Dickson G., Gower H.J., Barton C.H., Prentice H.M., Elsom V.L., Moore S.E.,
RA Cox R.D., Quinn C., Putt W., Walsh F.S.;
RT "Human muscle neural cell adhesion molecule (N-CAM): identification of a
RT muscle-specific sequence in the extracellular domain.";
RL Cell 50:1119-1130(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 501-858 (ISOFORM 5).
RX PubMed=3203385; DOI=10.1016/0092-8674(88)90241-3;
RA Gower H.J., Barton C.H., Elsom V.L., Thompson J., Moore S.E., Dickson G.,
RA Walsh F.S.;
RT "Alternative splicing generates a secreted form of N-CAM in muscle and
RT brain.";
RL Cell 55:955-964(1988).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RABIES VIRUS
RP GLYCOPROTEIN.
RX PubMed=9696812; DOI=10.1128/jvi.72.9.7181-7190.1998;
RA Thoulouze M.I., Lafage M., Schachner M., Hartmann U., Cremer H., Lafon M.;
RT "The neural cell adhesion molecule is a receptor for rabies virus.";
RL J. Virol. 72:7181-7190(1998).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-459.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ZIKA VIRUS ENVELOPE
RP PROTEIN E.
RX PubMed=32753727; DOI=10.1038/s41467-020-17638-y;
RA Srivastava M., Zhang Y., Chen J., Sirohi D., Miller A., Zhang Y., Chen Z.,
RA Lu H., Xu J., Kuhn R.J., Andy Tao W.;
RT "Chemical proteomics tracks virus entry and uncovers NCAM1 as Zika virus
RT receptor.";
RL Nat. Commun. 11:3896-3896(2020).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for rabies virus.
CC {ECO:0000269|PubMed:9696812}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Zika virus.
CC {ECO:0000269|PubMed:32753727}.
CC -!- SUBUNIT: (Microbial infection) Interacts with rabies virus
CC glycoprotein. {ECO:0000269|PubMed:9696812}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Zika virus envelope
CC protein E. {ECO:0000269|PubMed:32753727}.
CC -!- SUBUNIT: Interacts with MDK. {ECO:0000250|UniProtKB:P13595}.
CC -!- INTERACTION:
CC P13591; P25098: GRK2; NbExp=3; IntAct=EBI-2846607, EBI-3904795;
CC P13591; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-2846607, EBI-357085;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor, GPI-
CC anchor.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Lipid-
CC anchor, GPI-anchor {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P13591-2; Sequence=Displayed;
CC Name=2; Synonyms=N-CAM 140;
CC IsoId=P13591-1; Sequence=VSP_034818;
CC Name=3; Synonyms=N-CAM 120;
CC IsoId=P13591-3, P13592-2;
CC Sequence=VSP_034818, VSP_034822, VSP_034824, VSP_034825;
CC Name=4;
CC IsoId=P13591-4; Sequence=VSP_034818, VSP_034824, VSP_034825;
CC Name=5; Synonyms=C;
CC IsoId=P13591-5, P13592-1;
CC Sequence=VSP_034821, VSP_034823;
CC Name=6;
CC IsoId=P13591-6; Sequence=VSP_034819, VSP_034820;
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92680.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=NCAM entry;
CC URL="https://en.wikipedia.org/wiki/NCAM";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=N-CAM 140;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_264";
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DR EMBL; X16841; CAA34739.1; -; mRNA.
DR EMBL; U63041; AAB04558.1; -; mRNA.
DR EMBL; S71824; AAB31836.1; -; mRNA.
DR EMBL; AK292453; BAF85142.1; -; mRNA.
DR EMBL; AB209443; BAD92680.1; ALT_INIT; mRNA.
DR EMBL; BC014205; AAH14205.2; -; mRNA.
DR EMBL; BC029119; AAH29119.1; -; mRNA.
DR EMBL; BC047244; AAH47244.1; -; mRNA.
DR EMBL; S73101; AAB20698.1; -; mRNA.
DR EMBL; M17410; AAA59913.1; -; mRNA.
DR EMBL; M17409; AAA59912.1; -; mRNA.
DR EMBL; M22094; AAA59910.1; -; mRNA.
DR EMBL; M22092; AAA59911.1; -; Genomic_DNA.
DR EMBL; M22091; AAA59911.1; JOINED; Genomic_DNA.
DR CCDS; CCDS73385.1; -. [P13591-2]
DR CCDS; CCDS73386.1; -. [P13591-3]
DR CCDS; CCDS73387.1; -. [P13591-4]
DR CCDS; CCDS73388.1; -. [P13591-1]
DR PIR; A31635; A31635.
DR PIR; I54773; I54773.
DR PIR; S07784; IJHUNG.
DR RefSeq; NP_000606.3; NM_000615.6. [P13591-1]
DR RefSeq; NP_001070150.1; NM_001076682.3. [P13591-3]
DR RefSeq; NP_001229537.1; NM_001242608.1. [P13591-4]
DR RefSeq; NP_851996.2; NM_181351.4. [P13591-2]
DR PDB; 2E3V; X-ray; 1.95 A; A/B/C=510-619.
DR PDB; 2HAZ; X-ray; 1.70 A; A=508-608.
DR PDB; 2VKW; X-ray; 2.30 A; A/B=506-702.
DR PDB; 2VKX; X-ray; 2.70 A; A/B/C/D/E/F=506-702.
DR PDB; 3MTR; X-ray; 1.80 A; A/B=414-611.
DR PDB; 5AEA; X-ray; 1.90 A; A/B=20-116.
DR PDB; 5LKN; NMR; -; A=611-702.
DR PDBsum; 2E3V; -.
DR PDBsum; 2HAZ; -.
DR PDBsum; 2VKW; -.
DR PDBsum; 2VKX; -.
DR PDBsum; 3MTR; -.
DR PDBsum; 5AEA; -.
DR PDBsum; 5LKN; -.
DR AlphaFoldDB; P13591; -.
DR BMRB; P13591; -.
DR SMR; P13591; -.
DR BioGRID; 110764; 59.
DR DIP; DIP-59530N; -.
DR IntAct; P13591; 34.
DR MINT; P13591; -.
DR STRING; 9606.ENSP00000480132; -.
DR ChEMBL; CHEMBL3712938; -.
DR GlyConnect; 1545; 8 N-Linked glycans (1 site).
DR GlyGen; P13591; 6 sites, 10 N-linked glycans (1 site).
DR iPTMnet; P13591; -.
DR PhosphoSitePlus; P13591; -.
DR SwissPalm; P13591; -.
DR BioMuta; NCAM1; -.
DR DMDM; 205830665; -.
DR EPD; P13591; -.
DR jPOST; P13591; -.
DR MassIVE; P13591; -.
DR MaxQB; P13591; -.
DR PaxDb; P13591; -.
DR PeptideAtlas; P13591; -.
DR PRIDE; P13591; -.
DR ProteomicsDB; 52931; -. [P13591-2]
DR ProteomicsDB; 52932; -. [P13591-1]
DR ProteomicsDB; 52933; -. [P13591-3]
DR ProteomicsDB; 52934; -. [P13591-4]
DR ProteomicsDB; 52935; -. [P13591-5]
DR ProteomicsDB; 52936; -. [P13591-6]
DR ABCD; P13591; 1 sequenced antibody.
DR Antibodypedia; 4329; 3470 antibodies from 56 providers.
DR CPTC; P13591; 1 antibody.
DR DNASU; 4684; -.
DR Ensembl; ENST00000316851.12; ENSP00000318472.8; ENSG00000149294.17. [P13591-2]
DR Ensembl; ENST00000529356.5; ENSP00000482205.1; ENSG00000149294.17. [P13591-6]
DR Ensembl; ENST00000531044.5; ENSP00000484943.1; ENSG00000149294.17. [P13591-1]
DR Ensembl; ENST00000621128.4; ENSP00000481083.1; ENSG00000149294.17. [P13591-4]
DR Ensembl; ENST00000621850.4; ENSP00000480774.1; ENSG00000149294.17. [P13591-3]
DR GeneID; 4684; -.
DR KEGG; hsa:4684; -.
DR MANE-Select; ENST00000316851.12; ENSP00000318472.8; NM_181351.5; NP_851996.2.
DR UCSC; uc031yfh.2; human. [P13591-2]
DR CTD; 4684; -.
DR DisGeNET; 4684; -.
DR GeneCards; NCAM1; -.
DR HGNC; HGNC:7656; NCAM1.
DR HPA; ENSG00000149294; Tissue enhanced (brain, heart muscle).
DR MIM; 116930; gene.
DR neXtProt; NX_P13591; -.
DR OpenTargets; ENSG00000149294; -.
DR PharmGKB; PA31459; -.
DR VEuPathDB; HostDB:ENSG00000149294; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155743; -.
DR HOGENOM; CLU_068819_0_0_1; -.
DR InParanoid; P13591; -.
DR OMA; DSKQKGQ; -.
DR PhylomeDB; P13591; -.
DR TreeFam; TF326195; -.
DR PathwayCommons; P13591; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; P13591; -.
DR SIGNOR; P13591; -.
DR BioGRID-ORCS; 4684; 6 hits in 321 CRISPR screens.
DR ChiTaRS; NCAM1; human.
DR EvolutionaryTrace; P13591; -.
DR GeneWiki; Neural_cell_adhesion_molecule; -.
DR GenomeRNAi; 4684; -.
DR Pharos; P13591; Tbio.
DR PRO; PR:P13591; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P13591; protein.
DR Bgee; ENSG00000149294; Expressed in cortical plate and 196 other tissues.
DR ExpressionAtlas; P13591; baseline and differential.
DR Genevisible; P13591; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:ARUK-UCL.
DR GO; GO:2001260; P:regulation of semaphorin-plexin signaling pathway; ISS:ARUK-UCL.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
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; IPR033019; Ncam1.
DR InterPro; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231:SF239; PTHR12231:SF239; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; GPI-anchor;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..858
FT /note="Neural cell adhesion molecule 1"
FT /id="PRO_0000015009"
FT TOPO_DOM 20..718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..111
FT /note="Ig-like C2-type 1"
FT DOMAIN 116..205
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..301
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..413
FT /note="Ig-like C2-type 4"
FT DOMAIN 416..501
FT /note="Ig-like C2-type 5"
FT DOMAIN 509..608
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 611..706
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 766..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..96
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT DISULFID 139..189
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT DISULFID 235..287
FT /evidence="ECO:0000250|UniProtKB:P13590"
FT DISULFID 329..395
FT /evidence="ECO:0000305"
FT DISULFID 436..489
FT /evidence="ECO:0000305"
FT VAR_SEQ 354..363
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:1710251,
FT ECO:0000303|PubMed:2887295, ECO:0000303|PubMed:3253057,
FT ECO:0000303|PubMed:8075973, ECO:0000303|Ref.5"
FT /id="VSP_034818"
FT VAR_SEQ 364
FT /note="T -> V (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034819"
FT VAR_SEQ 365..858
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034820"
FT VAR_SEQ 609..665
FT /note="QGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEI
FT RLPSG -> HSPPPPASASSSTPVPLSPPDTTWPLPALATTEPAKNIAQNHCCNMFQAG
FT LHNALMK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:3203385"
FT /id="VSP_034821"
FT VAR_SEQ 609
FT /note="Q -> HSPPPPASASSSTPVPLSPPDTTWPLPALATTEPAK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:2887295,
FT ECO:0000303|PubMed:3253057"
FT /id="VSP_034822"
FT VAR_SEQ 666..858
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:3203385"
FT /id="VSP_034823"
FT VAR_SEQ 712..736
FT /note="NGSPTSGLSTGAIVGILIVIFVLLL -> TLGGNSASYTFVSLLFSAVTLLL
FT LC (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:2887295,
FT ECO:0000303|PubMed:3253057, ECO:0000303|Ref.5"
FT /id="VSP_034824"
FT VAR_SEQ 737..858
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:2887295,
FT ECO:0000303|PubMed:3253057, ECO:0000303|Ref.5"
FT /id="VSP_034825"
FT VARIANT 7
FT /note="L -> F (in dbSNP:rs7105734)"
FT /id="VAR_061331"
FT VARIANT 260
FT /note="D -> N (in dbSNP:rs17115160)"
FT /id="VAR_049960"
FT VARIANT 679
FT /note="E -> D (in dbSNP:rs17115280)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_049961"
FT VARIANT 834
FT /note="T -> M (in dbSNP:rs17174409)"
FT /id="VAR_049962"
FT CONFLICT 215
FT /note="Q -> R (in Ref. 2; AAB04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="G -> R (in Ref. 2; AAB04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="L -> F (in Ref. 2; AAB04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="Y -> H (in Ref. 4; BAF85142)"
FT /evidence="ECO:0000305"
FT CONFLICT 609..610
FT /note="QG -> R (in Ref. 8; AAA59913)"
FT /evidence="ECO:0000305"
FT CONFLICT 730..731
FT /note="Missing (in Ref. 8; AAA59913)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="G -> A (in Ref. 8; AAA59913)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="S -> N (in Ref. 6; AAH47244)"
FT /evidence="ECO:0000305"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5AEA"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:5AEA"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 432..442
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:3MTR"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 485..492
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 497..506
FT /evidence="ECO:0007829|PDB:3MTR"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:2HAZ"
FT HELIX 562..568
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 581..590
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:2HAZ"
FT STRAND 616..621
FT /evidence="ECO:0007829|PDB:2VKW"
FT STRAND 628..633
FT /evidence="ECO:0007829|PDB:2VKW"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:5LKN"
FT STRAND 644..651
FT /evidence="ECO:0007829|PDB:2VKW"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:2VKW"
FT STRAND 668..671
FT /evidence="ECO:0007829|PDB:2VKW"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:5LKN"
FT STRAND 679..688
FT /evidence="ECO:0007829|PDB:2VKW"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:2VKW"
FT LIPID P13591-3:741
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT LIPID P13591-4:706
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 858 AA; 94574 MW; FD3B9DE80D802554 CRC64;
MLQTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
KLTPNQQRIS VVWNDDSSST LTIYNANIDD AGIYKCVVTG EDGSESEATV NVKIFQKLMF
KNAPTPQEFR EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTIQARQNI VNATANLGQS VTLVCDAEGF
PEPTMSWTKD GEQIEQEEDD EKYIFSDDSS QLTIKKVDKN DEAEYICIAE NKAGEQDATI
HLKVFAKPKI TYVENQTAME LEEQVTLTCE ASGDPIPSIT WRTSTRNISS EEKASWTRPE
KQETLDGHMV VRSHARVSSL TLKSIQYTDA GEYICTASNT IGQDSQSMYL EVQYAPKLQG
PVAVYTWEGN QVNITCEVFA YPSATISWFR DGQLLPSSNY SNIKIYNTPS ASYLEVTPDS
ENDFGNYNCT AVNRIGQESL EFILVQADTP SSPSIDQVEP YSSTAQVQFD EPEATGGVPI
LKYKAEWRAV GEEVWHSKWY DAKEASMEGI VTIVGLKPET TYAVRLAALN GKGLGEISAA
SEFKTQPVQG EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVRYR ALSSEWKPEI
RLPSGSDHVM LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTSGLS
TGAIVGILIV IFVLLLVVVD ITCYFLNKCG LFMCIAVNLC GKAGPGAKGK DMEEGKAAFS
KDESKEPIVE VRTEEERTPN HDGGKHTEPN ETTPLTEPEK GPVEAKPECQ ETETKPAPAE
VKTVPNDATQ TKENESKA
