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Neuronal cell adhesion molecule (Nr-CAM) (Neuronal surface protein Bravo) (mBravo) (NgCAM-related cell adhesion molecule) (Ng-CAM-related)

 NRCAM_MOUSE             Reviewed;        1256 AA.
Q810U4; Q80U33; Q8BLG8; Q8BX92; Q8BYJ8;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
14-NOV-2003, sequence version 2.
12-SEP-2018, entry version 156.
RecName: Full=Neuronal cell adhesion molecule;
Short=Nr-CAM;
AltName: Full=Neuronal surface protein Bravo;
Short=mBravo;
AltName: Full=NgCAM-related cell adhesion molecule;
Short=Ng-CAM-related;
Flags: Precursor;
Name=Nrcam; Synonyms=Kiaa0343;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Swiss Webster; TISSUE=Brain;
Dirks P., Montag-Sallaz M., Montag D.;
"Expression patterns of L1-family cell recognition molecules L1, CHL1,
NrCAM, and neurofascin in the mouse brain.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1094-1256 (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
PROTEIN SEQUENCE OF 432-449 AND 705-723, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBUNIT.
PubMed=11564762; DOI=10.1083/jcb.200104122;
Sakurai T., Lustig M., Babiarz J., Furley A.J., Tait S., Brophy P.J.,
Brown S.A., Brown L.Y., Mason C.A., Grumet M.;
"Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in
cerebellar granule cell development.";
J. Cell Biol. 154:1259-1273(2001).
[6]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=14602817;
Custer A.W., Kazarinova-Noyes K., Sakurai T., Xu X., Simon W.,
Grumet M., Shrager P.;
"The role of the ankyrin-binding protein NrCAM in node of Ranvier
formation.";
J. Neurosci. 23:10032-10039(2003).
[7]
FUNCTION, AND INTERACTION WITH GLDN.
PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O.,
Spiegel I., Bermingham J.R. Jr., Peles E.;
"Gliomedin mediates Schwann cell-axon interaction and the molecular
assembly of the nodes of Ranvier.";
Neuron 47:215-229(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1173; TYR-1177;
SER-1178; SER-1203; SER-1206; SER-1242; SER-1243 AND SER-1247, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
TISSUE SPECIFICITY.
PubMed=20188654; DOI=10.1016/j.neuron.2010.02.004;
Feinberg K., Eshed-Eisenbach Y., Frechter S., Amor V., Salomon D.,
Sabanay H., Dupree J.L., Grumet M., Brophy P.J., Shrager P., Peles E.;
"A glial signal consisting of gliomedin and NrCAM clusters axonal Na+
channels during the formation of nodes of Ranvier.";
Neuron 65:490-502(2010).
[10]
INTERACTION WITH MYOC.
PubMed=23897819; DOI=10.1074/jbc.M112.446138;
Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
Tomarev S.I.;
"Myocilin mediates myelination in the peripheral nervous system
through ErbB2/3 signaling.";
J. Biol. Chem. 288:26357-26371(2013).
[11]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=24719088; DOI=10.1523/JNEUROSCI.4752-13.2014;
Amor V., Feinberg K., Eshed-Eisenbach Y., Vainshtein A., Frechter S.,
Grumet M., Rosenbluth J., Peles E.;
"Long-term maintenance of Na+ channels at nodes of Ranvier depends on
glial contact mediated by gliomedin and NrCAM.";
J. Neurosci. 34:5089-5098(2014).
-!- FUNCTION: Cell adhesion protein that is required for normal
responses to cell-cell contacts in brain and in the peripheral
nervous system. Plays a role in neurite outgrowth in response to
contactin binding (PubMed:11564762). Plays a role in mediating
cell-cell contacts between Schwann cells and axons
(PubMed:20188654). Plays a role in the formation and maintenance
of the nodes of Ranvier on myelinated axons. Nodes of Ranvier
contain clustered sodium channels that are crucial for the
saltatory propagation of action potentials along myelinated axons.
During development, nodes of Ranvier are formed by the fusion of
two heminodes. Required for normal clustering of sodium channels
at heminodes; not required for the formation of mature nodes with
normal sodium channel clusters (PubMed:14602817, PubMed:20188654).
Required, together with GLDN, for maintaining NFASC and sodium
channel clusters at mature nodes of Ranvier (PubMed:24719088).
{ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:14602817,
ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:20188654,
ECO:0000269|PubMed:24719088}.
-!- SUBUNIT: Constituent of a NFASC/NRCAM/ankyrin-G complex
(Probable). Detected in a complex with CNTN1 and PTPRB
(PubMed:11564762). Interacts with GLDN/gliomedin and MYOC
(PubMed:16039564, PubMed:23897819). {ECO:0000269|PubMed:11564762,
ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:23897819,
ECO:0000305|PubMed:20188654}.
-!- INTERACTION:
Q811D0:Dlg1; NbExp=6; IntAct=EBI-8321816, EBI-514290;
Q62108:Dlg4; NbExp=2; IntAct=EBI-8321816, EBI-300895;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20188654};
Single-pass type I membrane protein {ECO:0000305}. Cell
projection, axon {ECO:0000269|PubMed:14602817}. Secreted
{ECO:0000269|PubMed:20188654}. Note=Detected at nodes of Ranvier
(PubMed:14602817, PubMed:20188654, PubMed:24719088).
{ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:20188654,
ECO:0000269|PubMed:24719088}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q810U4-1; Sequence=Displayed;
Name=2;
IsoId=Q810U4-2; Sequence=VSP_008926, VSP_008927;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q810U4-3; Sequence=VSP_008930;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q810U4-4; Sequence=VSP_008923, VSP_008925;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q810U4-5; Sequence=VSP_008921, VSP_008922, VSP_008924;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in sciatic nerve (PubMed:14602817,
PubMed:20188654, PubMed:24719088). Detected in brain, especially
in the cerebellum Purkinje cell layer, inner granule cell layer
and molecular layer (at protein level) (PubMed:11564762). Detected
in neurons and Schwann cells (PubMed:20188654).
{ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:14602817,
ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate, are viable and fertile. They present no obvious phenotype
excepting subtle size differences of cerebellar lobes IV and V.
Contrary to wild-type, cerebellar cells do not form neurites when
plated on a surface coated with contactin (in vitro)
(PubMed:11564762). Neonates present delayed formation of sodium
channel clusters at developing nodes of Ranvier, but are
indistiguishable from wild-type at 10 days after birth
(PubMed:14602817, PubMed:20188654). Mice lacking both Gldn and
Nrcam are born at the expected Mendelian rate, but are smaller
than control littermates and display important neurological
impairments, in spite of seemingly normal nerve myelination. Motor
abnormalities vary between individuals, ranging from ataxia,
uncoordinated movements and premature death to weakness of the
hind limbs, hypomotility, strongly impaired ability to hang from a
horizontal bar with their forelimbs and a tendency to stumble. The
motor defects correlate with decreased velocity of nerve
conduction and slower propagation of action potentials. Most mice
die within 60 days after birth, and none are fertile. Mutant mice
display delayed formation of mature nodes of Ranvier; 15 days
after birth about 20% of the nodes lack detectable sodium channel
clusters. Sodium channel clustering and nerve conduction appear
normal 60 and 75 days after birth, but subsequently a gradual
disintegration of the nodal protein complexes is seen. About 70%
of the mutant nodes present high-density sodium channel clustering
at 120 days after birth, as opposed to nearly 100% for wild-type.
Contrary to wild-type, in adult nodes of Ranvier the sodium
channels are often clustered near the paranode border with an
empty gap in the middle. At nodes of Ranvier, Schwann cell
microvilli are sparse or absent and show defects in their
orientation, resulting in various structural abnormalities at the
node and the paranode border (PubMed:24719088).
{ECO:0000269|PubMed:11564762, ECO:0000269|PubMed:24719088}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
L1/neurofascin/NgCAM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAD65848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AJ543321; CAD65848.1; ALT_INIT; mRNA.
EMBL; AK122252; BAC65534.1; ALT_INIT; mRNA.
EMBL; AK039322; BAC30318.1; -; mRNA.
EMBL; AK048567; BAC33377.1; -; mRNA.
EMBL; AK045259; BAC32284.1; -; mRNA.
CCDS; CCDS49056.1; -. [Q810U4-1]
CCDS; CCDS49057.1; -. [Q810U4-2]
RefSeq; NP_001139503.1; NM_001146031.1. [Q810U4-2]
RefSeq; NP_795904.3; NM_176930.4. [Q810U4-1]
UniGene; Mm.208439; -.
ProteinModelPortal; Q810U4; -.
SMR; Q810U4; -.
BioGrid; 235320; 4.
IntAct; Q810U4; 5.
MINT; Q810U4; -.
STRING; 10090.ENSMUSP00000020939; -.
iPTMnet; Q810U4; -.
PhosphoSitePlus; Q810U4; -.
PaxDb; Q810U4; -.
PeptideAtlas; Q810U4; -.
PRIDE; Q810U4; -.
DNASU; 319504; -.
Ensembl; ENSMUST00000020939; ENSMUSP00000020939; ENSMUSG00000020598. [Q810U4-1]
Ensembl; ENSMUST00000110748; ENSMUSP00000106376; ENSMUSG00000020598. [Q810U4-2]
GeneID; 319504; -.
KEGG; mmu:319504; -.
UCSC; uc007nls.2; mouse. [Q810U4-5]
UCSC; uc007nlt.2; mouse. [Q810U4-2]
UCSC; uc007nlu.2; mouse. [Q810U4-1]
UCSC; uc007nlw.1; mouse. [Q810U4-4]
CTD; 4897; -.
MGI; MGI:104750; Nrcam.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000231380; -.
HOVERGEN; HBG000144; -.
InParanoid; Q810U4; -.
KO; K06756; -.
OMA; TLAEVHW; -.
OrthoDB; EOG091G00LY; -.
PhylomeDB; Q810U4; -.
TreeFam; TF351098; -.
Reactome; R-MMU-447043; Neurofascin interactions.
ChiTaRS; Nrcam; mouse.
PRO; PR:Q810U4; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020598; Expressed in 221 organ(s), highest expression level in pineal body.
CleanEx; MM_NRCAM; -.
ExpressionAtlas; Q810U4; baseline and differential.
Genevisible; Q810U4; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0043194; C:axon initial segment; ISO:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0030506; F:ankyrin binding; ISS:UniProtKB.
GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IGI:MGI.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
GO; GO:0007417; P:central nervous system development; IDA:UniProtKB.
GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:MGI.
GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
GO; GO:0008104; P:protein localization; IDA:MGI.
GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
Pfam; PF13882; Bravo_FIGEY; 1.
Pfam; PF00041; fn3; 4.
Pfam; PF07679; I-set; 2.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 6.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1256 Neuronal cell adhesion molecule.
/FTId=PRO_0000015058.
TOPO_DOM 30 1119 Extracellular. {ECO:0000255}.
TRANSMEM 1120 1142 Helical. {ECO:0000255}.
TOPO_DOM 1143 1256 Cytoplasmic. {ECO:0000255}.
DOMAIN 40 128 Ig-like C2-type 1.
DOMAIN 135 229 Ig-like C2-type 2.
DOMAIN 261 350 Ig-like C2-type 3.
DOMAIN 355 442 Ig-like C2-type 4.
DOMAIN 448 535 Ig-like C2-type 5.
DOMAIN 539 626 Ig-like C2-type 6.
DOMAIN 643 738 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 740 837 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 842 944 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 948 1045 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOD_RES 1173 1173 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1177 1177 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1178 1178 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1203 1203 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1206 1206 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000250|UniProtKB:P97686}.
MOD_RES 1242 1242 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1243 1243 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1247 1247 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 710 710 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 796 796 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 852 852 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 987 987 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1003 1003 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1013 1013 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1067 1067 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 62 117 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 161 212 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 286 334 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 376 426 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 470 519 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 561 610 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 35 35 D -> DPKLLHD (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008921.
VAR_SEQ 235 254 VDELNDTIAANLSDTEFYGA -> GKSSASGLSFNGVYLCG
SNY (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008922.
VAR_SEQ 254 259 AKSSKE -> GELQWL (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008923.
VAR_SEQ 255 1256 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008924.
VAR_SEQ 260 1256 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008925.
VAR_SEQ 629 638 Missing (in isoform 2).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_008926.
VAR_SEQ 1045 1107 AGIPPPDVGAGKGKEEWRKEIVNGSRSFFGLKGLMPGTAYK
VRVGAEGDSGFVSSEDVFETGP -> GKK (in isoform
2). {ECO:0000303|PubMed:12693553}.
/FTId=VSP_008927.
VAR_SEQ 1177 1177 Y -> YRSFE (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008930.
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


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