CD166_CARAU
ID CD166_CARAU Reviewed; 555 AA.
AC Q90304;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=CD166 antigen homolog;
DE AltName: Full=Activated leukocyte cell adhesion molecule;
DE AltName: Full=DM-GRASP homolog;
DE AltName: Full=Neurolin;
DE AltName: CD_antigen=CD166;
DE Flags: Precursor;
GN Name=alcam;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Laessing U.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-552, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Retina;
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:0000250|UniProtKB:Q61490}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q61490}. Note=Detected at the
CC immunological synapse, i.e, at the contact zone between antigen-
CC presenting dendritic cells and T-cells. Colocalizes with CD6 and the
CC TCR/CD3 complex at the immunological synapse.
CC {ECO:0000250|UniProtKB:Q13740}.
CC -!- TISSUE SPECIFICITY: Present on all retinal ganglion cells (RGCS) and
CC their axons (in embryo). Absent from mature axons along most of their
CC length, but is present on new and growing axons derived from the RGCS
CC at the retinal margin. Remains on adult RGCS only at cell-cell contact
CC sites and is continuously found in the retinal axon terminal arbor
CC layers of the adult tectum.
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; L25056; AAC38015.2; -; mRNA.
DR PIR; I50478; I50478.
DR AlphaFoldDB; Q90304; -.
DR BMRB; Q90304; -.
DR SMR; Q90304; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR013098; Ig_I-set.
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; PF07679; I-set; 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; 4.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell adhesion; Cell membrane; Cell projection;
KW Developmental protein; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..555
FT /note="CD166 antigen homolog"
FT /id="PRO_0000014664"
FT TOPO_DOM 23..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..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 319..397
FT /note="Ig-like C2-type 2"
FT DOMAIN 406..484
FT /note="Ig-like C2-type 3"
FT REGION 529..555
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 171
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"
SQ SEQUENCE 555 AA; 60372 MW; 5A4A8014F00BFF68 CRC64;
MQSVVCLIGA FIAAAVFRPG SCVGTVIGLY GETIVVPCND GTKKPDGLIF TKWKYVKDDG
SPGDLLVKQA QKDEATVSAT DGYKSRVSIA ANSSLLIARG SLADQRVFTC MVVSFTNLEE
YSVEVKVHKK PSAPVIKNNA KELENGKLTQ LGECVVENAN PPADLIWKKN NQTLVDDGKT
IIITSTITKD KITGLSSTSS RLQYTARKED VESQFTCTAK HVMGPDQVSE PESFPIHYPT
EKVSLQVVSQ SPIREGEDVT LKCQADGNPP PTSFNFNIKG KKVTVTDKDV YTLTGVTRAD
SGIYKCSLLD NDVMESTQFV TVSFLDVSLT PTGKVLKNVG ENLIVSLDKN ASSEAKVTWT
KDNRKLDKLP DFSKLTYSDA GLYVCDVSIE GIKRSLSFEL TVEGIPKITS LTKHRSSDGK
HKVLTCEAEG SPKPDVQWSV NGTNDEVSYN NGKATYKLTV VPSKNLTVSC LVTNKLGEDT
KEISVFSQKN EDGTEQAKVI VGIVVGLLVA AALVGLIYWI YIKKTRQGSW KTGEKEAGTS
EESKKLEENN HKPDV
