C166A_DANRE
ID C166A_DANRE Reviewed; 564 AA.
AC Q90460; Q90480;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=CD166 antigen homolog A;
DE AltName: Full=Activated leukocyte cell adhesion molecule A;
DE AltName: Full=DM-GRASP homolog {ECO:0000303|PubMed:8089660};
DE AltName: Full=Neurolin {ECO:0000303|PubMed:8026643};
DE AltName: CD_antigen=CD166;
DE Flags: Precursor;
GN Name=alcama; Synonyms=alcam, cd166;
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 SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=8089660; DOI=10.1002/neu.480250708;
RA Kanki J.P., Chang S., Kuwada J.Y.;
RT "The molecular cloning and characterization of potential chick DM-GRASP
RT homologs in zebrafish and mouse.";
RL J. Neurobiol. 25:831-845(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-561, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryo;
RX PubMed=8026643; DOI=10.1046/j.1432-0436.1994.56120021.x;
RA Laessing U., Giordano S., Stecher B., Lottspeich F., Stuermer C.A.O.;
RT "Molecular characterization of fish neurolin: a growth-associated cell
RT surface protein and member of the immunoglobulin superfamily in the fish
RT retinotectal system with similarities to chick protein DM-GRASP/SC-1/BEN.";
RL Differentiation 56:21-29(1994).
CC -!- FUNCTION: Cell adhesion molecule that mediates both heterotypic cell-
CC cell contacts via its interaction with CD6, as well as homotypic cell-
CC cell contacts. Promotes T-cell activation and proliferation via its
CC interactions with CD6 (By similarity). Contributes to the formation and
CC maturation of the immunological synapse via its interactions with CD6
CC (By similarity). Mediates homotypic interactions with cells that
CC express ALCAM. Mediates attachment of dendritic cells onto endothelial
CC cells via homotypic interaction. Inhibits endothelial cell migration
CC and promotes endothelial tube formation via homotypic interactions.
CC Required for normal organization of the lymph vessel network. Required
CC for normal hematopoietic stem cell engraftment in the bone marrow.
CC Plays a role in hematopoiesis; required for normal numbers of
CC hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast
CC proliferation and differentiation (By similarity). Promotes neurite
CC extension, axon growth and axon guidance; axons grow preferentially on
CC surfaces that contain ALCAM (By similarity). Mediates outgrowth and
CC pathfinding for retinal ganglion cell axons (By similarity).
CC {ECO:0000250|UniProtKB:P42292, ECO:0000250|UniProtKB:Q13740,
CC ECO:0000250|UniProtKB:Q61490}.
CC -!- SUBUNIT: Homodimer. Interacts (via extracellular domain) with CD6 (via
CC extracellular domain). Homodimerization and interaction with CD6
CC involve the same region and cannot occur simultaneously. The affinity
CC for CD6 is much higher than the affinity for self-association.
CC {ECO:0000250|UniProtKB:Q13740}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61490};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q61490}.
CC Cell projection, axon {ECO:0000269|PubMed:8026643,
CC ECO:0000269|PubMed:8089660}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q61490}. Note=Detected at the immunological
CC synapse, i.e, at the contact zone between antigen-presenting dendritic
CC cells and T-cells. Colocalizes with CD6 and the TCR/CD3 complex at the
CC immunological synapse. {ECO:0000250|UniProtKB:Q13740}.
CC -!- TISSUE SPECIFICITY: Expressed during axonogenesis in a subset of
CC developing sensory and motor neurons that fasciculate with each other
CC in the central nervous system (PubMed:8089660). Expressed in the
CC retinotectal system of both embryos and adults, with expression in all
CC retinal ganglion cells (RGC) during embryogenesis but only some RGCs in
CC adults (at protein level) (PubMed:8026643).
CC {ECO:0000269|PubMed:8026643, ECO:0000269|PubMed:8089660}.
CC -!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like
CC domain. {ECO:0000250|UniProtKB:Q13740}.
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DR EMBL; L25273; AAA50024.1; -; mRNA.
DR EMBL; L25057; AAA50048.1; -; mRNA.
DR RefSeq; NP_571075.1; NM_131000.1.
DR AlphaFoldDB; Q90460; -.
DR SMR; Q90460; -.
DR STRING; 7955.ENSDARP00000090957; -.
DR PaxDb; Q90460; -.
DR GeneID; 30194; -.
DR KEGG; dre:30194; -.
DR CTD; 30194; -.
DR ZFIN; ZDB-GENE-990415-30; alcama.
DR eggNOG; ENOG502RMQM; Eukaryota.
DR InParanoid; Q90460; -.
DR OrthoDB; 536204at2759; -.
DR PhylomeDB; Q90460; -.
DR PRO; PR:Q90460; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030424; C:axon; IDA:ZFIN.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0042802; F:identical protein binding; IDA:ZFIN.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN.
DR GO; GO:0060536; P:cartilage morphogenesis; IMP:CACAO.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0014033; P:neural crest cell differentiation; IMP:CACAO.
DR GO; GO:0030182; P:neuron differentiation; IMP:ZFIN.
DR GO; GO:0010770; P:positive regulation of cell morphogenesis involved in differentiation; IMP:CACAO.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR039810; CD166_antigen.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11973:SF2; PTHR11973:SF2; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell adhesion; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..564
FT /note="CD166 antigen homolog A"
FT /id="PRO_0000014663"
FT TOPO_DOM 25..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..127
FT /note="Ig-like V-type 1"
FT DOMAIN 131..229
FT /note="Ig-like V-type 2"
FT DOMAIN 239..323
FT /note="Ig-like C2-type 1"
FT DOMAIN 340..399
FT /note="Ig-like C2-type 2"
FT DOMAIN 406..484
FT /note="Ig-like C2-type 3"
FT REGION 539..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 426..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 488..497
FT /note="LFEEDKPKPG -> R (in Ref. 2; AAA50048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 61274 MW; ADAA7C293A607929 CRC64;
MHSVICLFGA FIAAALFAPG SCLPTVIGLY GETIEVPCNN GNNKPDGLIF TKWKYAKDDG
SPGDLLIKQA QKDDPTVSAM DGYKTRVSIA ANSSLLIAQG SLTDQRVFTC MVVSSTNLEE
FSVEVKVHKK PSAPVIKNKV KELENGKLTQ LGECVVESAN PAADLIWMKN NQALVDDGKT
IIITSDVTKD PVTGLSSTSS RLQYTARKED VASQFTCVAK HVTGPNQVST PDTFQIRYPT
EKVSLQVVSQ SPIREGDDVT LKCQADGNPP PTSFNFNIKG KKVTVTDKDV YTLTGVTRAD
SGVYKCSLLD NDVMESTQIV TVSFLDASLT PTGKVLKKLG ENLVVSLEKN ASSEVKVTWT
KDNRKLDKLP DFSQLRYSDA GLYVCDVSIE GIKHSFSFEL TVEGGPRITG LTKHRSNDGK
HKVLTCEAEG SPKPEVQWSV NGTDDETSYV NGKATYKLTV VPSKNLTVSC LVTNKLGFDT
KDISVFSLFE EDKPKPGKNE DGADQAKVIV GVVVGLFLAA ALVGLIYWLY IKKTRQGSWK
TGEKETGTSE ESKKLEENNH KADV
