NCHL1_MOUSE
ID NCHL1_MOUSE Reviewed; 1209 AA.
AC P70232; A2RRK1; Q8BS24; Q8C6W0; Q8C823; Q8VBY7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Neural cell adhesion molecule L1-like protein;
DE AltName: Full=Cell adhesion molecule with homology to L1CAM;
DE AltName: Full=Chl1-like protein;
DE AltName: Full=Close homolog of L1;
DE Contains:
DE RecName: Full=Processed neural cell adhesion molecule L1-like protein;
DE Flags: Precursor;
GN Name=Chl1; Synonyms=Call;
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), TISSUE SPECIFICITY, GLYCOSYLATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=8921253; DOI=10.1111/j.1460-9568.1996.tb01306.x;
RA Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H.,
RA Montag D., Schachner M.;
RT "Structural features of a close homologue of L1 (CHL1) in the mouse: a new
RT member of the L1 family of neural recognition molecules.";
RL Eur. J. Neurosci. 8:1613-1629(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Head, and Vein;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=129/Sv;
RX PubMed=12391163; DOI=10.1128/mcb.22.22.7967-7981.2002;
RA Montag-Sallaz M., Schachner M., Montag D.;
RT "Misguided axonal projections, neural cell adhesion molecule 180 mRNA
RT upregulation, and altered behavior in mice deficient for the close homolog
RT of L1.";
RL Mol. Cell. Biol. 22:7967-7981(2002).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, AND TISSUE
RP SPECIFICITY.
RX PubMed=10103075; DOI=10.1046/j.1460-9568.1999.00496.x;
RA Hillenbrand R., Molthagen M., Montag D., Schachner M.;
RT "The close homologue of the neural adhesion molecule L1 (CHL1): patterns of
RT expression and promotion of neurite outgrowth by heterophilic
RT interactions.";
RL Eur. J. Neurosci. 11:813-826(1999).
RN [8]
RP FUNCTION.
RX PubMed=10022583;
RX DOI=10.1002/(sici)1097-4695(19990215)38:3<428::aid-neu10>3.0.co;2-6;
RA Chen S., Mantei N., Dong L., Schachner M.;
RT "Prevention of neuronal cell death by neural adhesion molecules L1 and
RT CHL1.";
RL J. Neurobiol. 38:428-439(1999).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14659567; DOI=10.1016/s0166-4328(03)00114-1;
RA Pratte M., Rougon G., Schachner M., Jamon M.;
RT "Mice deficient for the close homologue of the neural adhesion cell L1
RT (CHL1) display alterations in emotional reactivity and motor
RT coordination.";
RL Behav. Brain Res. 147:31-39(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12812975; DOI=10.1093/hmg/ddg165;
RA Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J.,
RA Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K.,
RA D'Hooge R., De Deyn P.P., Froyen G.;
RT "CALL interrupted in a patient with non-specific mental retardation: gene
RT dosage-dependent alteration of murine brain development and behavior.";
RL Hum. Mol. Genet. 12:1463-1474(2003).
RN [11]
RP FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND ITGB1/ITGA2
RP HETERODIMER, MOTIFS, AND MUTAGENESIS OF 555-ASP--ALA-558 AND TYR-1186.
RX PubMed=12721290; DOI=10.1074/jbc.m303084200;
RA Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M., Maness P.F.;
RT "Close homolog of L1 is an enhancer of integrin-mediated cell migration.";
RL J. Biol. Chem. 278:25024-25031(2003).
RN [12]
RP FUNCTION, AND CLEAVAGE BY ADAM8.
RX PubMed=14761956; DOI=10.1074/jbc.m400560200;
RA Naus S., Richter M., Wildeboer D., Moss M., Schachner M., Bartsch J.W.;
RT "Ectodomain shedding of the neural recognition molecule CHL1 by the
RT metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses
RT neuronal cell death.";
RL J. Biol. Chem. 279:16083-16090(2004).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15504324; DOI=10.1016/j.neuron.2004.10.016;
RA Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J.,
RA Maness P.F.;
RT "Close homolog of L1 modulates area-specific neuronal positioning and
RT dendrite orientation in the cerebral cortex.";
RL Neuron 44:423-437(2004).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16623841; DOI=10.1111/j.1460-9568.2006.04710.x;
RA Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I.,
RA Irintchev A., Dityatev A., Schachner M.;
RT "Enhanced perisomatic inhibition and impaired long-term potentiation in the
RT CA1 region of juvenile CHL1-deficient mice.";
RL Eur. J. Neurosci. 23:1839-1852(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148; SER-1161 AND SER-1181,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [16]
RP CLEAVAGE BY BACE1.
RX PubMed=29325091; DOI=10.1093/jmcb/mjy001;
RA Wang X., Wang C., Pei G.;
RT "alpha-secretase ADAM10 physically interacts with beta-secretase BACE1 in
RT neurons and regulates CHL1 proteolysis.";
RL J. Mol. Cell Biol. 10:411-422(2018).
CC -!- FUNCTION: Extracellular matrix and cell adhesion protein that plays a
CC role in nervous system development and in synaptic plasticity. Both
CC soluble and membranous forms promote neurite outgrowth of cerebellar
CC and hippocampal neurons and suppress neuronal cell death. Plays a role
CC in neuronal positioning of pyramidal neurons as well as in regulation
CC of both the number of interneurons and the efficacy of GABAergic
CC synapses. May play a role in regulating cell migration in nerve
CC regeneration and cortical development. Potentiates integrin-dependent
CC cell migration towards extracellular matrix proteins. Recruits ANK3 to
CC the plasma membrane. {ECO:0000269|PubMed:10022583,
CC ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:12391163,
CC ECO:0000269|PubMed:12721290, ECO:0000269|PubMed:12812975,
CC ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:14761956,
CC ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:16623841}.
CC -!- SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1
CC heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.
CC -!- INTERACTION:
CC P70232; Q9JMB8: Cntn6; NbExp=5; IntAct=EBI-7703109, EBI-7703151;
CC P70232; P18052: Ptpra; NbExp=4; IntAct=EBI-7703109, EBI-6597520;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Soluble forms produced by cleavage/shedding also exist.
CC -!- SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like
CC protein]: Secreted, extracellular space, extracellular matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70232-2; Sequence=VSP_020083, VSP_020084, VSP_020085;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, in the cerebellum and in
CC the spinal cord. Detected in the retina and the optic nerve. Expressed
CC in neurons and glial cells in the central nervous system and by Schwann
CC cells in the peripheral nervous system. {ECO:0000269|PubMed:10103075,
CC ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:8921253}.
CC -!- DEVELOPMENTAL STAGE: Not detectable in the forebrain at 11 dpc, weakly
CC detectable at 13 dpc with highest detection at 18 dpc to postnatal day
CC 7. Down-regulated at postnatal day 15 and further reduced in four-week-
CC old animals. {ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:15504324,
CC ECO:0000269|PubMed:8921253}.
CC -!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment region.
CC -!- DOMAIN: The DGEA motif seems to be a recognition site for integrin.
CC -!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
CC generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
CC inhibited by metalloprotease inhibitors. In brain extracts, these two
CC soluble forms are also present and are dramatically reduced in mice
CC lacking ADAM8 (PubMed:14761956). Cleaved by BACE1 (PubMed:29325091).
CC {ECO:0000269|PubMed:14761956, ECO:0000269|PubMed:29325091}.
CC -!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated
CC carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc).
CC {ECO:0000269|PubMed:8921253}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:8921253}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit misguided axonal projections and
CC aberrant axonal connectivity. They show alterations of hippocampal
CC fiber organization and olfactory axon projections. Their exploratory
CC behavior in novel environments is altered suggesting deficits in
CC information processing and in attention. They also display signs of
CC decreased stress and are more sociable and less aggressive.
CC Heterozygous mice exhibit half levels of CHL1 expression in the
CC hippocampus compared to their wild-type littermates, reflecting a gene
CC dosage effect. {ECO:0000269|PubMed:12391163,
CC ECO:0000269|PubMed:12812975, ECO:0000269|PubMed:14659567,
CC ECO:0000269|PubMed:16623841}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30699.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X94310; CAA63972.1; -; mRNA.
DR EMBL; AK040765; BAC30699.1; ALT_FRAME; mRNA.
DR EMBL; AK048639; BAC33405.1; -; mRNA.
DR EMBL; AK053039; BAC35247.2; -; mRNA.
DR EMBL; AC153595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466523; EDK99388.1; -; Genomic_DNA.
DR EMBL; BC131670; AAI31671.1; -; mRNA.
DR EMBL; BC131671; AAI31672.1; -; mRNA.
DR EMBL; AJ319655; CAC88131.1; -; Genomic_DNA.
DR EMBL; AJ319656; CAC88131.1; JOINED; Genomic_DNA.
DR EMBL; AJ319657; CAC88131.1; JOINED; Genomic_DNA.
DR CCDS; CCDS39582.1; -. [P70232-1]
DR PIR; T42718; T42718.
DR RefSeq; NP_031723.2; NM_007697.2. [P70232-1]
DR RefSeq; XP_006505535.1; XM_006505472.3. [P70232-1]
DR RefSeq; XP_017176864.1; XM_017321375.1. [P70232-1]
DR RefSeq; XP_017176865.1; XM_017321376.1. [P70232-1]
DR AlphaFoldDB; P70232; -.
DR SMR; P70232; -.
DR BioGRID; 198702; 6.
DR IntAct; P70232; 2.
DR MINT; P70232; -.
DR STRING; 10090.ENSMUSP00000063933; -.
DR GlyConnect; 2538; 11 N-Linked glycans (5 sites).
DR GlyGen; P70232; 10 sites, 11 N-linked glycans (5 sites).
DR iPTMnet; P70232; -.
DR PhosphoSitePlus; P70232; -.
DR CPTAC; non-CPTAC-3993; -.
DR jPOST; P70232; -.
DR MaxQB; P70232; -.
DR PaxDb; P70232; -.
DR PeptideAtlas; P70232; -.
DR PRIDE; P70232; -.
DR ProteomicsDB; 252651; -. [P70232-1]
DR ProteomicsDB; 252652; -. [P70232-2]
DR ABCD; P70232; 2 sequenced antibodies.
DR Antibodypedia; 1160; 134 antibodies from 25 providers.
DR DNASU; 12661; -.
DR Ensembl; ENSMUST00000066905; ENSMUSP00000063933; ENSMUSG00000030077. [P70232-1]
DR Ensembl; ENSMUST00000203830; ENSMUSP00000144758; ENSMUSG00000030077. [P70232-1]
DR Ensembl; ENSMUST00000203912; ENSMUSP00000145026; ENSMUSG00000030077. [P70232-2]
DR GeneID; 12661; -.
DR KEGG; mmu:12661; -.
DR UCSC; uc009dcj.1; mouse. [P70232-1]
DR UCSC; uc009dck.1; mouse. [P70232-2]
DR CTD; 10752; -.
DR MGI; MGI:1098266; Chl1.
DR VEuPathDB; HostDB:ENSMUSG00000030077; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160080; -.
DR HOGENOM; CLU_005756_1_1_1; -.
DR InParanoid; P70232; -.
DR OMA; HETPPAX; -.
DR PhylomeDB; P70232; -.
DR TreeFam; TF351098; -.
DR BioGRID-ORCS; 12661; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Chl1; mouse.
DR PRO; PR:P70232; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70232; protein.
DR Bgee; ENSMUSG00000030077; Expressed in spermatid and 166 other tissues.
DR ExpressionAtlas; P70232; baseline and differential.
DR Genevisible; P70232; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050890; P:cognition; IMP:MGI.
DR GO; GO:0035640; P:exploration behavior; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA: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; 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; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1209
FT /note="Neural cell adhesion molecule L1-like protein"
FT /id="PRO_0000247897"
FT CHAIN 26..?
FT /note="Processed neural cell adhesion molecule L1-like
FT protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000314778"
FT TOPO_DOM 26..1083
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1084..1104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1105..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 235..328
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..417
FT /note="Ig-like C2-type 4"
FT DOMAIN 423..510
FT /note="Ig-like C2-type 5"
FT DOMAIN 515..607
FT /note="Ig-like C2-type 6"
FT DOMAIN 614..709
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 714..807
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 812..914
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 918..1015
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 696..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 555..558
FT /note="DGEA"
FT MOTIF 1182..1186
FT /note="FIG[AQ]Y"
FT COMPBIAS 1115..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 753..754
FT /note="Cleavage; by ADAM8"
FT SITE 1040..1041
FT /note="Cleavage; by ADAM8"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 445..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 536..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 227
FT /note="S -> LKHASDSSSSTEICSQA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020083"
FT VAR_SEQ 1016..1070
FT /note="SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETR
FT GRE -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020084"
FT VAR_SEQ 1138..1209
FT /note="SDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGA
FT KEKGSVESNGSSTATFPLRA -> RKMVLKQKLLSWSSSRGRTFYSCTKNTLFDGSSVD
FT MKTLQPLRYFSSNKHT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020085"
FT MUTAGEN 555..558
FT /note="DGEA->AGEV: Inhibition of migration potentiation."
FT /evidence="ECO:0000269|PubMed:12721290"
FT MUTAGEN 1186
FT /note="Y->A: Inhibition of migration potentiation."
FT /evidence="ECO:0000269|PubMed:12721290"
FT CONFLICT 50
FT /note="D -> G (in Ref. 2; BAC35247)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="D -> E (in Ref. 6; CAC88131)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="I -> V (in Ref. 2; BAC35247)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="E -> K (in Ref. 1; CAA63972)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="P -> G (in Ref. 1; CAA63972)"
FT /evidence="ECO:0000305"
SQ 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
