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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
 
 
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