ID   L1CA2_DANRE             Reviewed;         216 AA.
AC   Q90479;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Neural cell adhesion molecule L1.2;
DE            Short=N-CAM-L1.2;
DE            Short=NCAM-L1.2;
DE   Flags: Fragment;
GN   Name=nadl1.2;
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 many postmitotic neurons in 16-36
CC       hours embryos. Little or no expression in the olfactory placode, the
CC       anterior lateral line/acoustic ganglia complex, the posterior lateral
CC       line ganglion, late-developing hindbrain neurons and some Rohon-Beard
CC       cells in the spinal cord. {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; X89205; CAA61491.1; -; mRNA.
DR   AlphaFoldDB; Q90479; -.
DR   STRING; 7955.ENSDARP00000094506; -.
DR   PaxDb; Q90479; -.
DR   ZFIN; ZDB-GENE-990415-10; l1cama.
DR   eggNOG; KOG3513; Eukaryota.
DR   InParanoid; Q90479; -.
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:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008046; F:axon guidance receptor activity; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR   GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR   Pfam; PF13882; Bravo_FIGEY; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Cell projection; Developmental protein;
KW   Differentiation; Glycoprotein; Membrane; Neurogenesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..216
FT                   /note="Neural cell adhesion molecule L1.2"
FT                   /id="PRO_0000072706"
FT   TOPO_DOM        <1..73
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..64
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          127..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   216 AA;  24116 MW;  712B5101A3CF97AB CRC64;
     EFFIHYLRKD GPDKWEKSEK VNSTQSFYTL HGLQPGSQYR LKIDFNNTKW EQEIQTAGAR
     VMEVKSGFVT ESWFIGLISA LVLLLLVLLI LCFIKRSKGG KYSVKEKEEG QIDSEARPMN
     NEAFGEYRSL ESDNEEKRTA SQPSLCEDSK LCTDDGLDDY ANSNSVQTEV IMDESLASQS
     SGVRDVPDAE TQESSPLNPA TAISHHGLPN SAALLD