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Neural cell adhesion molecule L1-like protein (Cell adhesion molecule with homology to L1CAM) (Chl1-like protein) (Close homolog of L1) [Cleaved into: Processed neural cell adhesion molecule L1-like protein]

 NCHL1_MOUSE             Reviewed;        1209 AA.
P70232; A2RRK1; Q8BS24; Q8C6W0; Q8C823; Q8VBY7;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
12-SEP-2018, entry version 147.
RecName: Full=Neural cell adhesion molecule L1-like protein;
AltName: Full=Cell adhesion molecule with homology to L1CAM;
AltName: Full=Chl1-like protein;
AltName: Full=Close homolog of L1;
Contains:
RecName: Full=Processed neural cell adhesion molecule L1-like protein;
Flags: Precursor;
Name=Chl1; Synonyms=Call;
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), TISSUE SPECIFICITY,
GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
PubMed=8921253; DOI=10.1111/j.1460-9568.1996.tb01306.x;
Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H.,
Montag D., Schachner M.;
"Structural features of a close homologue of L1 (CHL1) in the mouse: a
new member of the L1 family of neural recognition molecules.";
Eur. J. Neurosci. 8:1613-1629(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Aorta, Head, and Vein;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, AND DISRUPTION
PHENOTYPE.
STRAIN=129/Sv;
PubMed=12391163; DOI=10.1128/MCB.22.22.7967-7981.2002;
Montag-Sallaz M., Schachner M., Montag D.;
"Misguided axonal projections, neural cell adhesion molecule 180 mRNA
upregulation, and altered behavior in mice deficient for the close
homolog of L1.";
Mol. Cell. Biol. 22:7967-7981(2002).
[7]
FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, AND TISSUE
SPECIFICITY.
PubMed=10103075; DOI=10.1046/j.1460-9568.1999.00496.x;
Hillenbrand R., Molthagen M., Montag D., Schachner M.;
"The close homologue of the neural adhesion molecule L1 (CHL1):
patterns of expression and promotion of neurite outgrowth by
heterophilic interactions.";
Eur. J. Neurosci. 11:813-826(1999).
[8]
FUNCTION.
PubMed=10022583;
DOI=10.1002/(SICI)1097-4695(19990215)38:3<428::AID-NEU10>3.0.CO;2-6;
Chen S., Mantei N., Dong L., Schachner M.;
"Prevention of neuronal cell death by neural adhesion molecules L1 and
CHL1.";
J. Neurobiol. 38:428-439(1999).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14659567; DOI=10.1016/S0166-4328(03)00114-1;
Pratte M., Rougon G., Schachner M., Jamon M.;
"Mice deficient for the close homologue of the neural adhesion cell L1
(CHL1) display alterations in emotional reactivity and motor
coordination.";
Behav. Brain Res. 147:31-39(2003).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12812975; DOI=10.1093/hmg/ddg165;
Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J.,
Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K.,
D'Hooge R., De Deyn P.P., Froyen G.;
"CALL interrupted in a patient with non-specific mental retardation:
gene dosage-dependent alteration of murine brain development and
behavior.";
Hum. Mol. Genet. 12:1463-1474(2003).
[11]
FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND
ITGB1/ITGA2 HETERODIMER, MOTIFS, AND MUTAGENESIS OF 555-ASP--ALA-558
AND TYR-1186.
PubMed=12721290; DOI=10.1074/jbc.M303084200;
Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M.,
Maness P.F.;
"Close homolog of L1 is an enhancer of integrin-mediated cell
migration.";
J. Biol. Chem. 278:25024-25031(2003).
[12]
FUNCTION, AND CLEAVAGE BY ADAM8.
PubMed=14761956; DOI=10.1074/jbc.M400560200;
Naus S., Richter M., Wildeboer D., Moss M., Schachner M.,
Bartsch J.W.;
"Ectodomain shedding of the neural recognition molecule CHL1 by the
metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and
suppresses neuronal cell death.";
J. Biol. Chem. 279:16083-16090(2004).
[13]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15504324; DOI=10.1016/j.neuron.2004.10.016;
Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J.,
Maness P.F.;
"Close homolog of L1 modulates area-specific neuronal positioning and
dendrite orientation in the cerebral cortex.";
Neuron 44:423-437(2004).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16623841; DOI=10.1111/j.1460-9568.2006.04710.x;
Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I.,
Irintchev A., Dityatev A., Schachner M.;
"Enhanced perisomatic inhibition and impaired long-term potentiation
in the CA1 region of juvenile CHL1-deficient mice.";
Eur. J. Neurosci. 23:1839-1852(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148; SER-1161 AND
SER-1181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
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).
-!- FUNCTION: Extracellular matrix and cell adhesion protein that
plays a role in nervous system development and in synaptic
plasticity. Both soluble and membranous forms promote neurite
outgrowth of cerebellar and hippocampal neurons and suppress
neuronal cell death. Plays a role in neuronal positioning of
pyramidal neurons as well as in regulation of both the number of
interneurons and the efficacy of GABAergic synapses. May play a
role in regulating cell migration in nerve regeneration and
cortical development. Potentiates integrin-dependent cell
migration towards extracellular matrix proteins. Recruits ANK3 to
the plasma membrane. {ECO:0000269|PubMed:10022583,
ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:12391163,
ECO:0000269|PubMed:12721290, ECO:0000269|PubMed:12812975,
ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:14761956,
ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:16623841}.
-!- SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1
heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.
-!- INTERACTION:
Q9JMB8:Cntn6; NbExp=5; IntAct=EBI-7703109, EBI-7703151;
P18052:Ptpra; NbExp=4; IntAct=EBI-7703109, EBI-6597520;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=Soluble forms produced by cleavage/shedding also
exist.
-!- SUBCELLULAR LOCATION: Processed neural cell adhesion molecule L1-
like protein: Secreted, extracellular space, extracellular matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70232-1; Sequence=Displayed;
Name=2;
IsoId=P70232-2; Sequence=VSP_020083, VSP_020084, VSP_020085;
-!- TISSUE SPECIFICITY: Expressed in the brain, in the cerebellum and
in the spinal cord. Detected in the retina and the optic nerve.
Expressed in neurons and glial cells in the central nervous system
and by Schwann cells in the peripheral nervous system.
{ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:15504324,
ECO:0000269|PubMed:8921253}.
-!- DEVELOPMENTAL STAGE: Not detectable in the forebrain at E11,
weakly detectable at E13 with highest detection at E18 to
postnatal day 7. Down-regulated at postnatal day 15 and further
reduced in four-week-old animals. {ECO:0000269|PubMed:10103075,
ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:8921253}.
-!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment
region.
-!- DOMAIN: The DGEA motif seems to be a recognition site for
integrin.
-!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
inhibited by metalloprotease inhibitors. In brain extracts, these
two soluble forms are also present and are dramatically reduced in
mice lacking ADAM8.
-!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a
sulfated carbohydrate structure type HNK-1 (SO4-3-
GlcUABeta1,3GalBeta1,4GlcNAc). {ECO:0000269|PubMed:8921253}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:8921253}.
-!- DISRUPTION PHENOTYPE: Mice exhibit misguided axonal projections
and aberrant axonal connectivity. They show alterations of
hippocampal fiber organization and olfactory axon projections.
Their exploratory behavior in novel environments is altered
suggesting deficits in information processing and in attention.
They also display signs of decreased stress and are more sociable
and less aggressive. Heterozygous mice exhibit half levels of CHL1
expression in the hippocampus compared to their wild-type
littermates, reflecting a gene dosage effect.
{ECO:0000269|PubMed:12391163, ECO:0000269|PubMed:12812975,
ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:16623841}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
L1/neurofascin/NgCAM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC30699.1; Type=Frameshift; Positions=616, 624, 631, 632, 642, 645; Evidence={ECO:0000305};
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EMBL; X94310; CAA63972.1; -; mRNA.
EMBL; AK040765; BAC30699.1; ALT_FRAME; mRNA.
EMBL; AK048639; BAC33405.1; -; mRNA.
EMBL; AK053039; BAC35247.2; -; mRNA.
EMBL; AC153595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC153598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC161824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466523; EDK99388.1; -; Genomic_DNA.
EMBL; BC131670; AAI31671.1; -; mRNA.
EMBL; BC131671; AAI31672.1; -; mRNA.
EMBL; AJ319655; CAC88131.1; -; Genomic_DNA.
EMBL; AJ319656; CAC88131.1; JOINED; Genomic_DNA.
EMBL; AJ319657; CAC88131.1; JOINED; Genomic_DNA.
CCDS; CCDS39582.1; -. [P70232-1]
PIR; T42718; T42718.
RefSeq; NP_031723.2; NM_007697.2. [P70232-1]
RefSeq; XP_006505535.1; XM_006505472.3. [P70232-1]
RefSeq; XP_017176864.1; XM_017321375.1. [P70232-1]
RefSeq; XP_017176865.1; XM_017321376.1. [P70232-1]
UniGene; Mm.251288; -.
ProteinModelPortal; P70232; -.
SMR; P70232; -.
BioGrid; 198702; 1.
IntAct; P70232; 3.
MINT; P70232; -.
STRING; 10090.ENSMUSP00000063933; -.
iPTMnet; P70232; -.
PhosphoSitePlus; P70232; -.
MaxQB; P70232; -.
PaxDb; P70232; -.
PeptideAtlas; P70232; -.
PRIDE; P70232; -.
Ensembl; ENSMUST00000066905; ENSMUSP00000063933; ENSMUSG00000030077. [P70232-1]
Ensembl; ENSMUST00000203830; ENSMUSP00000144758; ENSMUSG00000030077. [P70232-1]
Ensembl; ENSMUST00000203912; ENSMUSP00000145026; ENSMUSG00000030077. [P70232-2]
GeneID; 12661; -.
KEGG; mmu:12661; -.
UCSC; uc009dcj.1; mouse. [P70232-1]
UCSC; uc009dck.1; mouse. [P70232-2]
CTD; 10752; -.
MGI; MGI:1098266; Chl1.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000231380; -.
HOVERGEN; HBG000144; -.
InParanoid; P70232; -.
KO; K06758; -.
OMA; YVRYQFR; -.
OrthoDB; EOG091G00LY; -.
TreeFam; TF351098; -.
PRO; PR:P70232; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030077; Expressed in 204 organ(s), highest expression level in Ammon's horn.
CleanEx; MM_CHL1; -.
ExpressionAtlas; P70232; baseline and differential.
Genevisible; P70232; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0050890; P:cognition; IMP:MGI.
GO; GO:0035640; P:exploration behavior; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IDA: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; 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.
Pfam; PF13895; Ig_2; 1.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
Extracellular matrix; Glycoprotein; Immunoglobulin domain; Membrane;
Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1209 Neural cell adhesion molecule L1-like
protein.
/FTId=PRO_0000247897.
CHAIN 26 ? Processed neural cell adhesion molecule
L1-like protein. {ECO:0000255}.
/FTId=PRO_0000314778.
TOPO_DOM 26 1083 Extracellular. {ECO:0000255}.
TRANSMEM 1084 1104 Helical. {ECO:0000255}.
TOPO_DOM 1105 1209 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 124 Ig-like C2-type 1.
DOMAIN 128 223 Ig-like C2-type 2.
DOMAIN 235 328 Ig-like C2-type 3.
DOMAIN 331 417 Ig-like C2-type 4.
DOMAIN 423 510 Ig-like C2-type 5.
DOMAIN 515 607 Ig-like C2-type 6.
DOMAIN 614 709 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 714 807 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 812 914 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 918 1015 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 555 558 DGEA.
MOTIF 1182 1186 FIG[AQ]Y.
SITE 753 754 Cleavage; by ADAM8.
SITE 1040 1041 Cleavage; by ADAM8.
MOD_RES 1148 1148 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1161 1161 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1181 1181 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 562 562 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 767 767 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 822 822 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1027 1027 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 153 204 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 262 310 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 352 401 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 445 494 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 536 591 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 227 227 S -> LKHASDSSSSTEICSQA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020083.
VAR_SEQ 1016 1070 SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDN
DSIFQDVIETRGRE -> K (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020084.
VAR_SEQ 1138 1209 SDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNE
DGSFIGAYTGAKEKGSVESNGSSTATFPLRA -> RKMVLK
QKLLSWSSSRGRTFYSCTKNTLFDGSSVDMKTLQPLRYFSS
NKHT (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020085.
MUTAGEN 555 558 DGEA->AGEV: Inhibition of migration
potentiation.
{ECO:0000269|PubMed:12721290}.
MUTAGEN 1186 1186 Y->A: Inhibition of migration
potentiation.
{ECO:0000269|PubMed:12721290}.
CONFLICT 50 50 D -> G (in Ref. 2; BAC35247).
{ECO:0000305}.
CONFLICT 77 77 D -> E (in Ref. 6; CAC88131).
{ECO:0000305}.
CONFLICT 425 425 I -> V (in Ref. 2; BAC35247).
{ECO:0000305}.
CONFLICT 602 602 E -> K (in Ref. 1; CAA63972).
{ECO:0000305}.
CONFLICT 612 612 P -> G (in Ref. 1; CAA63972).
{ECO:0000305}.
SEQUENCE 1209 AA; 135074 MW; 2C689475920AB84C CRC64;
MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK
GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS
EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP
PAQMGSLSAK TVLKGDTLLL ECFAEGLPTP HIQWSKPGSE LPEGRATIEV HEKTLKIENI
SYQDRGNYRC TANNLLGKAS HDFHVTVEEP PRWKKKPQSA VYSTGSSGIL LCEAEGEPQP
TIKWRLNGLP IEKHPFPGDF MFPREISFTN LLPNHTGVYQ CEASNIHGTI LANANIDVID
VIPLIKTKNE ENYATVVGYS AFLHCEYFAS PKATVVWEVA DETHPLEGDR YHTHENGTLE
IYRTTEEDAG SYSCWVDNAM GKAVITANLD IRNATKLRVS PKNPRIPKSH VLELYCESQC
DSHLKHSLKL SWSKDGEAFE MNGTEDGRIV IDGAYLTISN ITAEDQGVYS CSAQTSLDST
SEKTQVTVLG VPDPPGNLHL SERQNRSVRL SWEAGDDHNS KISEYIVEFE GNREEPGKWE
ELTRVQGEET DVVLSLAPYV RYQFRVTAVN EVGRSHASLP SDHHETPPAA PDKNPQNIRV
QASQPKEMII KWEPLKSMEQ NGPGLEYKVS WKPQGAPEEW EEEIVTNHTL RVMTPTVYAP
YDVKVQAINQ LGSSPDPQPV TLYSGEDYPS TAPVIQRVDV MNSTLVKVTW SSIPKETVHG
LLRGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDPFSEFHL TVLAYNSKGA
GPESEPYIFQ TPEGVPEQPS FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY
ELGELNEINV TTPSKSSWHL SNLNSTTKYK FYLRACTSRG CGKPISEEGA TLGEGSKGIR
KITEGVNVTQ KIHPVEVLVP GAEHIVHLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST
QGWFIGLMCA IALLTLILLT ICFVKRNRGG KYSVKEKEDL HPDPEVQSAK DETFGEYSDS
DEKPLKGSLR SLNRNMQPTE SADSLVEYGE GDQSIFNEDG SFIGAYTGAK EKGSVESNGS
STATFPLRA


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