NCAM1_MOUSE
ID NCAM1_MOUSE Reviewed; 1115 AA.
AC P13595; P13594; Q61949; Q61950; Q6LBU8; Q8BQ96; Q8C4B2; Q921P2; Q9R2A7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 209.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=3595563; DOI=10.1002/j.1460-2075.1987.tb04837.x;
RA Barthels D., Santoni M.-J., Wille W., Ruppert C., Chaix J.-C.,
RA Hirsch M.-R., Fontecilla-Camps J.-C., Goridis C.;
RT "Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a Mr
RT 79,000 polypeptide without a membrane-spanning region.";
RL EMBO J. 6:907-914(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1106 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-700 AND 702-1115 (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=2721486; DOI=10.1002/j.1460-2075.1989.tb03389.x;
RA Santoni M.J., Barthels D., Vopper G., Boned A., Goridis C., Wille W.;
RT "Differential exon usage involving an unusual splicing mechanism generates
RT at least eight types of NCAM cDNA in mouse brain.";
RL EMBO J. 8:385-392(1989).
RN [5]
RP PROTEIN SEQUENCE OF 20-36.
RX PubMed=3512556; DOI=10.1016/s0021-9258(17)35796-4;
RA Rougon G., Marshak D.R.;
RT "Structural and immunological characterization of the amino-terminal domain
RT of mammalian neural cell adhesion molecules.";
RL J. Biol. Chem. 261:3396-3401(1986).
RN [6]
RP PROTEIN SEQUENCE OF 38-48; 122-152; 166-177; 555-572; 584-595; 607-619;
RP 652-662 AND 685-691, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 529-1115 (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=3684567; DOI=10.1093/nar/15.21.8621;
RA Santoni M.-J., Barthels D., Barbas J.A., Hirsch M.-R., Steinmetz M.,
RA Goridis C., Wille W.;
RT "Analysis of cDNA clones that code for the transmembrane forms of the mouse
RT neural cell adhesion molecule (NCAM) and are generated by alternative RNA
RT splicing.";
RL Nucleic Acids Res. 15:8621-8641(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 642-1115.
RX PubMed=3396534; DOI=10.1002/j.1460-2075.1988.tb02856.x;
RA Barbas J.A., Chaix J.-C., Steinmetz M., Goridis C.;
RT "Differential splicing and alternative polyadenylation generates distinct
RT NCAM transcripts and proteins in the mouse.";
RL EMBO J. 7:625-632(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 804-1081 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=2454455; DOI=10.1093/nar/16.10.4217;
RA Barthels D., Vopper G., Wille W.;
RT "NCAM-180, the large isoform of the neural cell adhesion molecule of the
RT mouse, is encoded by an alternatively spliced transcript.";
RL Nucleic Acids Res. 16:4217-4225(1988).
RN [10]
RP INTERACTION WITH MDK.
RX PubMed=10772929; DOI=10.1006/bbrc.2000.2549;
RA Muramatsu H., Zou K., Sakaguchi N., Ikematsu S., Sakuma S., Muramatsu T.;
RT "LDL receptor-related protein as a component of the midkine receptor.";
RL Biochem. Biophys. Res. Commun. 270:936-941(2000).
RN [11]
RP GLYCOSYLATION AT ASN-222; ASN-316; ASN-348; ASN-424; ASN-450 AND ASN-479,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=14658030; DOI=10.1007/s00216-003-2383-2;
RA Albach C., Damoc E., Denzinger T., Schachner M., Przybylski M., Schmitz B.;
RT "Identification of N-glycosylation sites of the murine neural cell adhesion
RT molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry.";
RL Anal. Bioanal. Chem. 378:1129-1135(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-946; SER-958 AND SER-1005,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770; SER-774; SER-887;
RP SER-890; SER-926; THR-929; SER-946; SER-958; THR-1001; SER-1005 AND
RP THR-1030, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP STRUCTURE BY NMR OF 20-116, AND DISULFIDE BONDS.
RX PubMed=8673600; DOI=10.1038/nsb0796-581;
RA Thomsen N.K., Soroka V., Jensen P.H., Berezin V., Kiselyov V.V., Bock E.,
RA Poulsen F.M.;
RT "The three-dimensional structure of the first domain of neural cell
RT adhesion molecule.";
RL Nat. Struct. Biol. 3:581-585(1996).
RN [18]
RP STRUCTURE BY NMR OF 119-208, AND DISULFIDE BONDS.
RX PubMed=10331878; DOI=10.1038/8292;
RA Jensen P.H., Soroka V., Thomsen N.K., Ralets I., Berezin V., Bock E.,
RA Poulsen F.M.;
RT "Structure and interactions of NCAM modules 1 and 2, basic elements in
RT neural cell adhesion.";
RL Nat. Struct. Biol. 6:486-493(1999).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC -!- SUBUNIT: Interacts with MDK. {ECO:0000269|PubMed:10772929}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=N-CAM 180;
CC IsoId=P13595-1; Sequence=Displayed;
CC Name=2; Synonyms=N-CAM 140;
CC IsoId=P13595-2; Sequence=VSP_002588;
CC Name=3; Synonyms=N-CAM 120;
CC IsoId=P13595-3, P13594-1;
CC Sequence=VSP_034828, VSP_034829;
CC Name=4;
CC IsoId=P13595-4; Sequence=VSP_034826, VSP_034827;
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DR EMBL; Y00051; CAA68263.1; -; mRNA.
DR EMBL; BC011310; AAH11310.1; -; mRNA.
DR EMBL; AK051197; BAC34554.2; -; mRNA.
DR EMBL; AK082621; BAC38551.2; -; mRNA.
DR EMBL; X15049; CAA33148.1; -; mRNA.
DR EMBL; X15051; CAA33150.1; -; mRNA.
DR EMBL; X15052; CAA33151.1; -; mRNA.
DR EMBL; X06328; CAA29641.1; -; mRNA.
DR EMBL; X07195; CAA30173.1; -; Genomic_DNA.
DR EMBL; X07197; CAA30175.1; -; Genomic_DNA.
DR EMBL; X07198; CAB40820.1; -; Genomic_DNA.
DR EMBL; X07200; CAA30177.1; -; Genomic_DNA.
DR EMBL; X07244; CAA30230.1; -; mRNA.
DR CCDS; CCDS40617.1; -. [P13595-2]
DR CCDS; CCDS40618.1; -. [P13595-3]
DR PIR; A29673; IJMSNL.
DR RefSeq; NP_001074914.1; NM_001081445.1.
DR RefSeq; NP_001106675.1; NM_001113204.1.
DR RefSeq; NP_001297994.1; NM_001311065.1.
DR RefSeq; NP_035005.2; NM_010875.3.
DR PDB; 2NCM; NMR; -; A=20-116.
DR PDB; 3NCM; NMR; -; A=119-208.
DR PDBsum; 2NCM; -.
DR PDBsum; 3NCM; -.
DR AlphaFoldDB; P13595; -.
DR BMRB; P13595; -.
DR SMR; P13595; -.
DR BioGRID; 201699; 19.
DR CORUM; P13595; -.
DR IntAct; P13595; 7.
DR MINT; P13595; -.
DR STRING; 10090.ENSMUSP00000130668; -.
DR GlyConnect; 2535; 6 N-Linked glycans (3 sites).
DR GlyGen; P13595; 6 sites, 6 N-linked glycans (3 sites).
DR iPTMnet; P13595; -.
DR PhosphoSitePlus; P13595; -.
DR SwissPalm; P13595; -.
DR CPTAC; non-CPTAC-3846; -.
DR jPOST; P13595; -.
DR MaxQB; P13595; -.
DR PaxDb; P13595; -.
DR PeptideAtlas; P13595; -.
DR PRIDE; P13595; -.
DR ProteomicsDB; 287445; -. [P13595-1]
DR ProteomicsDB; 287446; -. [P13595-2]
DR ProteomicsDB; 287447; -. [P13595-3]
DR ProteomicsDB; 287448; -. [P13595-4]
DR DNASU; 17967; -.
DR GeneID; 17967; -.
DR KEGG; mmu:17967; -.
DR UCSC; uc009pje.2; mouse. [P13595-1]
DR CTD; 4684; -.
DR MGI; MGI:97281; Ncam1.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; P13595; -.
DR OrthoDB; 129648at2759; -.
DR PhylomeDB; P13595; -.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR BioGRID-ORCS; 17967; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ncam1; mouse.
DR EvolutionaryTrace; P13595; -.
DR PRO; PR:P13595; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P13595; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0030275; F:LRR domain binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0071679; P:commissural neuron axon guidance; IGI:ARUK-UCL.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0033555; P:multicellular organismal response to stress; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0048666; P:neuron development; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0001928; P:regulation of exocyst assembly; IMP:MGI.
DR GO; GO:2001260; P:regulation of semaphorin-plexin signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR GO; GO:0010288; P:response to lead ion; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0021794; P:thalamus development; ISO:MGI.
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; IPR013106; Ig_V-set.
DR InterPro; IPR033019; Ncam1.
DR InterPro; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231:SF239; PTHR12231:SF239; 1.
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 SMART; SM00406; IGv; 2.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Heparin-binding; Immunoglobulin domain; Lipoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3512556"
FT CHAIN 20..1115
FT /note="Neural cell adhesion molecule 1"
FT /id="PRO_0000015012"
FT TOPO_DOM 20..711
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..1115
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..302
FT /note="Ig-like C2-type 3"
FT DOMAIN 309..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 407..492
FT /note="Ig-like C2-type 5"
FT DOMAIN 500..599
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 601..696
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 756..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..156
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT BINDING 161..165
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 929
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1001
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1030
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:14658030"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14658030"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14658030"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14658030"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14658030,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14658030"
FT DISULFID 41..96
FT /evidence="ECO:0000269|PubMed:8673600,
FT ECO:0007744|PDB:2NCM"
FT DISULFID 139..189
FT /evidence="ECO:0000269|PubMed:10331878,
FT ECO:0007744|PDB:3NCM"
FT DISULFID 235..288
FT /evidence="ECO:0000305"
FT DISULFID 330..386
FT /evidence="ECO:0000305"
FT DISULFID 427..480
FT /evidence="ECO:0000305"
FT VAR_SEQ 601..605
FT /note="EPSAP -> KSSLF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034826"
FT VAR_SEQ 606..1115
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034827"
FT VAR_SEQ 702..725
FT /note="NGSPTAGLSTGAIVGILIVIFVLL -> TLGGSSTSYTLVSLLFSAVTLLLL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:3595563"
FT /id="VSP_034828"
FT VAR_SEQ 726..1115
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:3595563"
FT /id="VSP_034829"
FT VAR_SEQ 810..1076
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:2721486, ECO:0000303|PubMed:3684567"
FT /id="VSP_002588"
FT CONFLICT 20
FT /note="L -> M (in Ref. 4; CAA33148)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> F (in Ref. 2; AAH11310)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..268
FT /note="DEKHIFSD -> ERSRSSVS (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> V (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..355
FT /note="KT -> QD (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> R (in Ref. 1; CAA68263 and 4; CAA33148)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> M (in Ref. 1; CAA68263 and 4; CAA33148)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="MY -> ID (in Ref. 1; CAA68263 and 4; CAA33148)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="F -> V (in Ref. 2; AAH11310 and 3; BAC34554/
FT BAC38551)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="K -> T (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="R -> T (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="V -> D (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 589..594
FT /note="SAATEF -> MQPSES (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 600..602
FT /note="REP -> PEL (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="D -> H (in Ref. 1; CAA68263)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="C -> W (in Ref. 3; BAC34554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="T -> A (in Ref. 3; BAC34554)"
FT /evidence="ECO:0000305"
FT STRAND 21..32
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2NCM"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2NCM"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:2NCM"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:3NCM"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:3NCM"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:3NCM"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:3NCM"
FT LIPID P13595-3:706
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1115 AA; 119427 MW; 78AF831BABD23918 CRC64;
MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF
KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF
PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS
IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM
VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG
NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC
TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS
LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR
EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM
LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS TGAIVGILIV
IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE
VRTEEERTPN HDGGKHTEPN ETTPLTEPEL PADTTATVED MLPSVTTVTT NSDTITETFA
TAQNSPTSET TTLTSSIAPP ATTVPDSNSV PAGQATPSKG VTASSSSPAS APKVAPLVDL
SDTPTSAPSA SNLSSTVLAN QGAVLSPSTP ASAGETSKAP PASKASPAPT PTPAGAASPL
AAVAAPATDA PQAKQEAPST KGPDPEPTQP GTVKNPPEAA TAPASPKSKA ATTNPSQGED
LKMDEGNFKT PDIDLAKDVF AALGSPRPAT GASGQASELA PSPADSAVPP APAKTEKGPV
ETKSEPPESE AKPAPTEVKT VPNDATQTKE NESKA
