NRCAM_MOUSE
ID NRCAM_MOUSE Reviewed; 1256 AA.
AC Q810U4; Q80U33; Q8BLG8; Q8BX92; Q8BYJ8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Neuronal cell adhesion molecule;
DE Short=Nr-CAM;
DE AltName: Full=Neuronal surface protein Bravo;
DE Short=mBravo;
DE AltName: Full=NgCAM-related cell adhesion molecule;
DE Short=Ng-CAM-related;
DE Flags: Precursor;
GN Name=Nrcam; Synonyms=Kiaa0343;
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 1).
RC STRAIN=Swiss Webster; TISSUE=Brain;
RA Dirks P., Montag-Sallaz M., Montag D.;
RT "Expression patterns of L1-family cell recognition molecules L1, CHL1,
RT NrCAM, and neurofascin in the mouse brain.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1094-1256 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 PROTEIN SEQUENCE OF 432-449 AND 705-723, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=11564762; DOI=10.1083/jcb.200104122;
RA Sakurai T., Lustig M., Babiarz J., Furley A.J., Tait S., Brophy P.J.,
RA Brown S.A., Brown L.Y., Mason C.A., Grumet M.;
RT "Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in
RT cerebellar granule cell development.";
RL J. Cell Biol. 154:1259-1273(2001).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14602817; DOI=10.1523/jneurosci.23-31-10032.2003;
RA Custer A.W., Kazarinova-Noyes K., Sakurai T., Xu X., Simon W., Grumet M.,
RA Shrager P.;
RT "The role of the ankyrin-binding protein NrCAM in node of Ranvier
RT formation.";
RL J. Neurosci. 23:10032-10039(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH GLDN.
RX PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
RA Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I.,
RA Bermingham J.R. Jr., Peles E.;
RT "Gliomedin mediates Schwann cell-axon interaction and the molecular
RT assembly of the nodes of Ranvier.";
RL Neuron 47:215-229(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1173; TYR-1177; SER-1178;
RP SER-1203; SER-1206; SER-1242; SER-1243 AND SER-1247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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 [9]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=20188654; DOI=10.1016/j.neuron.2010.02.004;
RA Feinberg K., Eshed-Eisenbach Y., Frechter S., Amor V., Salomon D.,
RA Sabanay H., Dupree J.L., Grumet M., Brophy P.J., Shrager P., Peles E.;
RT "A glial signal consisting of gliomedin and NrCAM clusters axonal Na+
RT channels during the formation of nodes of Ranvier.";
RL Neuron 65:490-502(2010).
RN [10]
RP INTERACTION WITH MYOC.
RX PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA Tomarev S.I.;
RT "Myocilin mediates myelination in the peripheral nervous system through
RT ErbB2/3 signaling.";
RL J. Biol. Chem. 288:26357-26371(2013).
RN [11]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24719088; DOI=10.1523/jneurosci.4752-13.2014;
RA Amor V., Feinberg K., Eshed-Eisenbach Y., Vainshtein A., Frechter S.,
RA Grumet M., Rosenbluth J., Peles E.;
RT "Long-term maintenance of Na+ channels at nodes of Ranvier depends on glial
RT contact mediated by gliomedin and NrCAM.";
RL J. Neurosci. 34:5089-5098(2014).
CC -!- FUNCTION: Cell adhesion protein that is required for normal responses
CC to cell-cell contacts in brain and in the peripheral nervous system.
CC Plays a role in neurite outgrowth in response to contactin binding
CC (PubMed:11564762). Plays a role in mediating cell-cell contacts between
CC Schwann cells and axons (PubMed:20188654). Plays a role in the
CC formation and maintenance of the nodes of Ranvier on myelinated axons.
CC Nodes of Ranvier contain clustered sodium channels that are crucial for
CC the saltatory propagation of action potentials along myelinated axons.
CC During development, nodes of Ranvier are formed by the fusion of two
CC heminodes. Required for normal clustering of sodium channels at
CC heminodes; not required for the formation of mature nodes with normal
CC sodium channel clusters (PubMed:14602817, PubMed:20188654). Required,
CC together with GLDN, for maintaining NFASC and sodium channel clusters
CC at mature nodes of Ranvier (PubMed:24719088).
CC {ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:14602817,
CC ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:20188654,
CC ECO:0000269|PubMed:24719088}.
CC -!- SUBUNIT: Constituent of a NFASC/NRCAM/ankyrin-G complex (Probable).
CC Detected in a complex with CNTN1 and PTPRB (PubMed:11564762). Interacts
CC with GLDN/gliomedin and MYOC (PubMed:16039564, PubMed:23897819).
CC {ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:16039564,
CC ECO:0000269|PubMed:23897819, ECO:0000305|PubMed:20188654}.
CC -!- INTERACTION:
CC Q810U4; Q811D0: Dlg1; NbExp=6; IntAct=EBI-8321816, EBI-514290;
CC Q810U4; Q62108: Dlg4; NbExp=2; IntAct=EBI-8321816, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20188654};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC axon {ECO:0000269|PubMed:14602817}. Secreted
CC {ECO:0000269|PubMed:20188654}. Note=Detected at nodes of Ranvier
CC (PubMed:14602817, PubMed:20188654, PubMed:24719088).
CC {ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:20188654,
CC ECO:0000269|PubMed:24719088}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q810U4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q810U4-2; Sequence=VSP_008926, VSP_008927;
CC Name=3;
CC IsoId=Q810U4-3; Sequence=VSP_008930;
CC Name=4;
CC IsoId=Q810U4-4; Sequence=VSP_008923, VSP_008925;
CC Name=5;
CC IsoId=Q810U4-5; Sequence=VSP_008921, VSP_008922, VSP_008924;
CC -!- TISSUE SPECIFICITY: Detected in sciatic nerve (PubMed:14602817,
CC PubMed:20188654, PubMed:24719088). Detected in brain, especially in the
CC cerebellum Purkinje cell layer, inner granule cell layer and molecular
CC layer (at protein level) (PubMed:11564762). Detected in neurons and
CC Schwann cells (PubMed:20188654). {ECO:0000269|PubMed:11564762,
CC ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:20188654,
CC ECO:0000269|PubMed:24719088}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, are
CC viable and fertile. They present no obvious phenotype excepting subtle
CC size differences of cerebellar lobes IV and V. Contrary to wild-type,
CC cerebellar cells do not form neurites when plated on a surface coated
CC with contactin (in vitro) (PubMed:11564762). Neonates present delayed
CC formation of sodium channel clusters at developing nodes of Ranvier,
CC but are indistiguishable from wild-type at 10 days after birth
CC (PubMed:14602817, PubMed:20188654). Mice lacking both Gldn and Nrcam
CC are born at the expected Mendelian rate, but are smaller than control
CC littermates and display important neurological impairments, in spite of
CC seemingly normal nerve myelination. Motor abnormalities vary between
CC individuals, ranging from ataxia, uncoordinated movements and premature
CC death to weakness of the hind limbs, hypomotility, strongly impaired
CC ability to hang from a horizontal bar with their forelimbs and a
CC tendency to stumble. The motor defects correlate with decreased
CC velocity of nerve conduction and slower propagation of action
CC potentials. Most mice die within 60 days after birth, and none are
CC fertile. Mutant mice display delayed formation of mature nodes of
CC Ranvier; 15 days after birth about 20% of the nodes lack detectable
CC sodium channel clusters. Sodium channel clustering and nerve conduction
CC appear normal 60 and 75 days after birth, but subsequently a gradual
CC disintegration of the nodal protein complexes is seen. About 70% of the
CC mutant nodes present high-density sodium channel clustering at 120 days
CC after birth, as opposed to nearly 100% for wild-type. Contrary to wild-
CC type, in adult nodes of Ranvier the sodium channels are often clustered
CC near the paranode border with an empty gap in the middle. At nodes of
CC Ranvier, Schwann cell microvilli are sparse or absent and show defects
CC in their orientation, resulting in various structural abnormalities at
CC the node and the paranode border (PubMed:24719088).
CC {ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:24719088}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD65848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ543321; CAD65848.1; ALT_INIT; mRNA.
DR EMBL; AK122252; BAC65534.1; ALT_INIT; mRNA.
DR EMBL; AK039322; BAC30318.1; -; mRNA.
DR EMBL; AK048567; BAC33377.1; -; mRNA.
DR EMBL; AK045259; BAC32284.1; -; mRNA.
DR CCDS; CCDS49056.1; -. [Q810U4-1]
DR CCDS; CCDS49057.1; -. [Q810U4-2]
DR RefSeq; NP_001139503.1; NM_001146031.1. [Q810U4-2]
DR RefSeq; NP_795904.3; NM_176930.4. [Q810U4-1]
DR AlphaFoldDB; Q810U4; -.
DR SMR; Q810U4; -.
DR BioGRID; 235320; 12.
DR CORUM; Q810U4; -.
DR IntAct; Q810U4; 4.
DR MINT; Q810U4; -.
DR STRING; 10090.ENSMUSP00000020939; -.
DR GlyConnect; 2549; 30 N-Linked glycans (11 sites).
DR GlyGen; Q810U4; 17 sites, 28 N-linked glycans (11 sites).
DR iPTMnet; Q810U4; -.
DR PhosphoSitePlus; Q810U4; -.
DR MaxQB; Q810U4; -.
DR PaxDb; Q810U4; -.
DR PeptideAtlas; Q810U4; -.
DR PRIDE; Q810U4; -.
DR ProteomicsDB; 253105; -. [Q810U4-1]
DR ProteomicsDB; 253106; -. [Q810U4-2]
DR ProteomicsDB; 253107; -. [Q810U4-3]
DR ProteomicsDB; 253108; -. [Q810U4-4]
DR ProteomicsDB; 253109; -. [Q810U4-5]
DR ABCD; Q810U4; 19 sequenced antibodies.
DR Antibodypedia; 17285; 361 antibodies from 39 providers.
DR DNASU; 319504; -.
DR Ensembl; ENSMUST00000020939; ENSMUSP00000020939; ENSMUSG00000020598. [Q810U4-1]
DR Ensembl; ENSMUST00000110748; ENSMUSP00000106376; ENSMUSG00000020598. [Q810U4-2]
DR GeneID; 319504; -.
DR KEGG; mmu:319504; -.
DR UCSC; uc007nls.2; mouse. [Q810U4-5]
DR UCSC; uc007nlt.2; mouse. [Q810U4-2]
DR UCSC; uc007nlu.2; mouse. [Q810U4-1]
DR UCSC; uc007nlw.1; mouse. [Q810U4-4]
DR CTD; 4897; -.
DR MGI; MGI:104750; Nrcam.
DR VEuPathDB; HostDB:ENSMUSG00000020598; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155419; -.
DR HOGENOM; CLU_005756_1_1_1; -.
DR InParanoid; Q810U4; -.
DR OMA; MVQPPTI; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; Q810U4; -.
DR TreeFam; TF351098; -.
DR BioGRID-ORCS; 319504; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nrcam; mouse.
DR PRO; PR:Q810U4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q810U4; protein.
DR Bgee; ENSMUSG00000020598; Expressed in epithelium of lens and 198 other tissues.
DR ExpressionAtlas; Q810U4; baseline and differential.
DR Genevisible; Q810U4; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043194; C:axon initial segment; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0033268; C:node of Ranvier; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0030506; F:ankyrin binding; ISS:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IGI:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IDA:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:MGI.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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; IPR003006; Ig/MHC_CS.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1256
FT /note="Neuronal cell adhesion molecule"
FT /id="PRO_0000015058"
FT TOPO_DOM 30..1119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1120..1142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1143..1256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 261..350
FT /note="Ig-like C2-type 3"
FT DOMAIN 355..442
FT /note="Ig-like C2-type 4"
FT DOMAIN 448..535
FT /note="Ig-like C2-type 5"
FT DOMAIN 539..626
FT /note="Ig-like C2-type 6"
FT DOMAIN 643..738
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 740..837
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 842..944
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 948..1045
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1151..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1173
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97686"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1013
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 161..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 286..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 376..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 470..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 561..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 35
FT /note="D -> DPKLLHD (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008921"
FT VAR_SEQ 235..254
FT /note="VDELNDTIAANLSDTEFYGA -> GKSSASGLSFNGVYLCGSNY (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008922"
FT VAR_SEQ 254..259
FT /note="AKSSKE -> GELQWL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008923"
FT VAR_SEQ 255..1256
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008924"
FT VAR_SEQ 260..1256
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008925"
FT VAR_SEQ 629..638
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_008926"
FT VAR_SEQ 1045..1107
FT /note="AGIPPPDVGAGKGKEEWRKEIVNGSRSFFGLKGLMPGTAYKVRVGAEGDSGF
FT VSSEDVFETGP -> GKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_008927"
FT VAR_SEQ 1177
FT /note="Y -> YRSFE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008930"
SQ SEQUENCE 1256 AA; 138522 MW; F3F698C2AF3FCFFA CRC64;
MQLKIMPKKK HLSAGGVPLI LFLCQMISAL DVPLDLVQPP TITQQSPKDY IIDPRENIVI
QCEAKGKPPP SFSWTRNGTH FDIDKDPLVT MKPGSGTLVI NIMSEGKAET YEGVYQCTAR
NERGAAVSNN IVVRPSRSPL WTKERLEPIV LQNGQSLVLP CRPPIGLPPA IIFWMDNSFQ
RLPQSERVSQ GLNGDLYFSN VLPEDTREDY ICYARFNHTQ TIQQKQPISL KVISVDELND
TIAANLSDTE FYGAKSSKER PPTFLTPEGN ESHKEELRGN VLSLECIAEG LPTPIIYWIK
EDGMLPANRT FYRNFKKTLQ ITHVSEADSG NYQCIAKNAL GAVHHTISVT VKAAPYWIVA
PQNLVLSPGE NGTLICRANG NPKPRISWLT NGVPIEIALD DPSRKIDGDT IIFSNVQESS
SAVYQCNASN KYGYLLANAF VNVLAEPPRI LTSANTLYQV IANRPALLDC AFFGSPMPTI
EWFKGTKGSA LHEDIYVLHD NGTLEIPVAQ KDSTGTYTCV ARNKLGMAKN EVHLEIKDPT
RIIKQPEYAV VQRGSKVSFE CRVKHDHTLI PTIMWLKDNG ELPNDERFST DKDHLVVSDV
KDDDGGTYTC TANTTLDSAS ASAVLRVVAP TPTPAPIYDV PNPPFDLELT NQLDKSVQLT
WTPGDDNNSP ITKFIIEYED AMHDAGLWRH QAEVSGTQTT AQLKLSPYVN YSFRVMAENS
IGRSMPSEAS EQYLTKAAEP DQNPMAVEGL GTEPDNLVIT WKPLNGFQSN GPGLQYKVSW
RQKDGDDEWT SVVVANVSKY IVSGTPTFVP YLIKVQALND VGFAPEPAAV MGHSGEDLPM
VAPGNVRVSV VNSTLAEVHW DPVPPKSVRG HLQGYRIYYW KTQSSSKRNR RHIEKKILTF
QGTKTHGMLP GLQPYSHYAL NVRVVNGKGE GPASTDRGFH TPEGVPSAPS SLKIVNPTLD
SLTLEWDPPS HPNGILTEYI LQYQPINSTH ELGPLVDLKI PANKTRWTLK NLNFSTRYKF
YFYAQTSVGP GSQITEEAIT TVDEAGIPPP DVGAGKGKEE WRKEIVNGSR SFFGLKGLMP
GTAYKVRVGA EGDSGFVSSE DVFETGPAMA SRQVDIATQG WFIGLMCAVA LLILILLIVC
FIRRNKGGKY PVKEKEDAHA DPEIQPMKED DGTFGEYSDA EDHKPLKKGS RTPSDRTVKK
EDSDDSLVDY GEGVNGQFNE DGSFIGQYSG KKEKEPAEGN ESSEAPSPVN AMNSFV
