L1CA1_DANRE
ID L1CA1_DANRE Reviewed; 1197 AA.
AC Q90478;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Neural cell adhesion molecule L1.1;
DE Short=N-CAM-L1.1;
DE Short=NCAM-L1.1;
DE Flags: Fragment;
GN Name=nadl1.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8568941; DOI=10.1002/jnr.490420413;
RA Tongiorgi E., Bernhardt R.R., Schachner M.;
RT "Zebrafish neurons express two L1-related molecules during early
RT axonogenesis.";
RL J. Neurosci. Res. 42:547-561(1995).
CC -!- FUNCTION: Cell adhesion molecule with an important role in the
CC development of the nervous system. Involved in neuron-neuron adhesion,
CC neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on
CC neurons (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell projection, growth cone {ECO:0000250|UniProtKB:Q05695}.
CC -!- TISSUE SPECIFICITY: Expressed in postmitotic neurons in 16-36 hours
CC embryos, including those in the brain, cranial ganglia and otic and
CC olfactory placodes, and in all classes of spinal neurons.
CC {ECO:0000269|PubMed:8568941}.
CC -!- DEVELOPMENTAL STAGE: Onset of expression correlates with the initiation
CC of axonogenesis in 16-36 hours embryos. {ECO:0000269|PubMed:8568941}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR EMBL; X89204; CAA61490.1; -; mRNA.
DR PIR; T30581; T30581.
DR AlphaFoldDB; Q90478; -.
DR SMR; Q90478; -.
DR STRING; 7955.ENSDARP00000121175; -.
DR PaxDb; Q90478; -.
DR PRIDE; Q90478; -.
DR ZFIN; ZDB-GENE-980526-512; l1camb.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; Q90478; -.
DR PhylomeDB; Q90478; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0031103; P:axon regeneration; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0060536; P:cartilage morphogenesis; IGI:CACAO.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IMP:ZFIN.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 11.
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 Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Cell projection; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurogenesis; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..1197
FT /note="Neural cell adhesion molecule L1.1"
FT /id="PRO_0000072705"
FT TOPO_DOM <1..1054
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1076..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN <1..58
FT /note="Ig-like C2-type 1"
FT DOMAIN 69..160
FT /note="Ig-like C2-type 2"
FT DOMAIN 165..263
FT /note="Ig-like C2-type 3"
FT DOMAIN 268..355
FT /note="Ig-like C2-type 4"
FT DOMAIN 360..442
FT /note="Ig-like C2-type 5"
FT DOMAIN 451..541
FT /note="Ig-like C2-type 6"
FT DOMAIN 548..643
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 645..742
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 747..852
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 853..952
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 953..1048
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 630..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
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 92..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 199..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 289..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 383..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 472..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 1197 AA; 132861 MW; 7CE1505EEFAC7B28 CRC64;
EFRQRDPSPS FRWVKDGKQF GEVLSESGTL TPHPTMDLHF YQGTYRCYAA NELGTAVSNL
VHLTTEPVPS LAKVKKQKRR AYEVGESAVL RCNPPKSSVT PKIHWMDMQF HHIPLNERVT
ISRDGNLYFA NLIANDSRDD YTCNAHYINA SIILPKEPMS IYVTPSNSVV KNRRAKLHHP
AGARSSYLVL RGQTLTLQCI PEGLPTPEVH WDRIDSALSP NRTKKLYNNR WLQIDNVLES
DDGEYVCTAR NSENSVKHHY TVTVEAAPYW TRSPEEHLYA PGETVRLDCK ADGIPAPNIT
WSINGVPVSG TDVDPRRRVS SGKLILSNVE FSDTAVYQCE AVNKHGSILI NTHVHVVELP
AQILTPDERL YQATAGQTVM LDCRTFGSPL PKIHWEILDS IPALSNAKIS QTTNGSLKIS
NVSEEDSNRY TCSVSETNKS ISADVEVLNR TKIVGPPQNL HVIRGSDAIL HCKYTVDHNL
KSPTVQWNKD GHKITASTSN DKYHEIEGSL KVLDVQMEDM GIYSCEVSTT LDSDTASGYI
TVQDKPDPPQ SLKLSEKMER SVTISWMPSV ENNSPVTEYV IEMNEGETPD EGQWQKYRSV
SQDIDSWRSI CSYSKYHFQI RAVNSIGTSA PTESSLSYST PAAKPDTNPE NVMTLSTDPK
SMIISWQEMD RRQFNGPGFQ YKVFWRRAAD SGAHWTESSV SNPPLMVNNT GTFVSFEIKV
QAVNDLGAAP EPLTVIGYSG EDFPLEAPSA LSVTELQKTS VMVRWSPVRP ESVRGHLLGY
KIYLRMKGSQ WETPGRAVSS SGNPTVIEVP ADAAEKIVSD LQFYSDYTLT ITAFNSKGEG
PHSEESFSTP EGAPGPVLFL PFDSPSESEI TLRWEAPHKP NGEIRGYLLQ YQEVVIGSES
PQHVESIDLP AVTEFTLKNL NPESRYTFHL SARNDAGDGA PAIQSGATLL DGEPPSVINM
TAGETSVNLS WVPGDRHRNL GFSFRYLKKI EGAEWEESEK INSTQAFYQL QGLDSGVIYH
LQVLSGNTSY DWDFKTIYSP EWHKSPRNFA TEGWFIGLIS ALVLLLLVLL LLCYIKKSKG
GKYSVKDKEE GQGDAANQKL KDDAFGEYRS LESDMEKCSI SQPSGCESKR SSNDSLADYG
DSVDIQFNED GSFIGQYSGR RDPRGHDSSG AVSPVNPNMP PPSHSFPTSV TGILGPN
