CD166_CHICK
ID CD166_CHICK Reviewed; 588 AA.
AC P42292;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=CD166 antigen;
DE AltName: Full=Activated leukocyte cell adhesion molecule;
DE AltName: Full=BEN glycoprotein {ECO:0000303|PubMed:1313497, ECO:0000303|PubMed:1608932};
DE AltName: Full=Protein DM-GRASP {ECO:0000303|PubMed:1873027};
DE AltName: Full=Protein JC7;
DE AltName: Full=SC1 glycoprotein;
DE AltName: CD_antigen=CD166;
DE Flags: Precursor;
GN Name=ALCAM;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF 34-53,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1931049; DOI=10.1016/0896-6273(91)90366-8;
RA Tanaka H., Matsui T., Agata A., Tomura M., Kubota I., McFarland K.C.,
RA Kohr B., Lee A., Phillips H.S., Shelton D.L.;
RT "Molecular cloning and expression of a novel adhesion molecule, SC1.";
RL Neuron 7:535-545(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RX PubMed=1873027; DOI=10.1016/0896-6273(91)90259-3;
RA Burns F.R., von Kannen S., Guy L., Raper J.A., Kamholz J., Chang S.;
RT "DM-GRASP, a novel immunoglobulin superfamily axonal surface protein that
RT supports neurite extension.";
RL Neuron 7:209-220(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-52; 87-93; 504-512 AND
RP 569-582, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Bursa of Fabricius;
RX PubMed=1608932; DOI=10.1073/pnas.89.12.5261;
RA Pourquie O., Corbel C., Le Caer J.-P., Rossier J., le Douarin N.M.;
RT "BEN, a surface glycoprotein of the immunoglobulin superfamily, is
RT expressed in a variety of developing systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5261-5265(1992).
RN [4]
RP POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1313497; DOI=10.1523/jneurosci.12-04-01548.1992;
RA Pourquie O., Hallonet M.E.R., le Douarin N.M.;
RT "Association of BEN glycoprotein expression with climbing fiber
RT axonogenesis in the avian cerebellum.";
RL J. Neurosci. 12:1548-1557(1992).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22421359; DOI=10.1242/jcs.096149;
RA Thelen K., Maier B., Faber M., Albrecht C., Fischer P., Pollerberg G.E.;
RT "Translation of the cell adhesion molecule ALCAM in axonal growth cones
RT - regulation and functional importance.";
RL J. Cell Sci. 125:1003-1014(2012).
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 (PubMed:1931049, PubMed:22421359). Mediates attachment of
CC dendritic cells onto endothelial cells via homotypic interaction.
CC Inhibits endothelial cell migration and promotes endothelial tube
CC formation via homotypic interactions. Required for normal organization
CC of the lymph vessel network. Required for normal hematopoietic stem
CC cell engraftment in the bone marrow. Plays a role in hematopoiesis;
CC required for normal numbers of hematopoietic stem cells in bone marrow.
CC Promotes in vitro osteoblast proliferation and differentiation (By
CC similarity). Promotes neurite extension, axon growth and axon guidance;
CC axons grow preferentially on surfaces that contain ALCAM
CC (PubMed:1873027, PubMed:22421359). Mediates outgrowth and pathfinding
CC for retinal ganglion cell axons (PubMed:22421359).
CC {ECO:0000250|UniProtKB:Q13740, ECO:0000250|UniProtKB:Q61490,
CC ECO:0000269|PubMed:1873027, ECO:0000269|PubMed:1931049,
CC ECO:0000269|PubMed:22421359}.
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:0000269|PubMed:1608932,
CC ECO:0000269|PubMed:1873027, ECO:0000269|PubMed:1931049,
CC ECO:0000269|PubMed:22421359}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q61490}. Cell projection, axon
CC {ECO:0000269|PubMed:1873027, ECO:0000269|PubMed:22421359}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q61490}. Note=Detected at
CC the 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: Detected in embryo (PubMed:1931049,
CC PubMed:1608932). Detected in embryonic spinal cord and embryonic brain
CC (PubMed:1873027, PubMed:1313497). Within the spinal cord it is
CC localized to axons in the dorsal funiculus, midline floor plate cells,
CC and motoneurons (PubMed:1873027). Detected in embryonic epithelia and
CC brain (PubMed:1608932). After hatching, detected in bursa of Fabricius
CC and thymus (PubMed:1608932). Detected on embryonic retinal ganglion
CC cell axon growth cones (at protein level) (PubMed:22421359). Detected
CC in embryonic retina and in the optic fiber layer, which is composed of
CC retinal ganglion cell axons and their growth cones (PubMed:22421359).
CC {ECO:0000269|PubMed:1313497, ECO:0000269|PubMed:1608932,
CC ECO:0000269|PubMed:1873027, ECO:0000269|PubMed:1931049,
CC ECO:0000269|PubMed:22421359}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic development.
CC {ECO:0000269|PubMed:1608932, ECO:0000269|PubMed:1931049}.
CC -!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like
CC domain. {ECO:0000250|UniProtKB:Q13740}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1608932,
CC ECO:0000269|PubMed:1873027}.
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DR EMBL; S63276; AAB20170.1; -; mRNA.
DR EMBL; M76678; AAA48602.1; -; mRNA.
DR EMBL; X64301; CAA45579.1; -; mRNA.
DR PIR; A45254; A45254.
DR PIR; JH0464; JH0464.
DR PIR; JH0506; JH0506.
DR RefSeq; NP_990510.1; NM_205179.1.
DR AlphaFoldDB; P42292; -.
DR SMR; P42292; -.
DR STRING; 9031.ENSGALP00000024723; -.
DR PaxDb; P42292; -.
DR Ensembl; ENSGALT00000024769; ENSGALP00000024723; ENSGALG00000015348.
DR GeneID; 396092; -.
DR KEGG; gga:396092; -.
DR CTD; 214; -.
DR VEuPathDB; HostDB:geneid_396092; -.
DR eggNOG; ENOG502RMQM; Eukaryota.
DR GeneTree; ENSGT00940000156881; -.
DR HOGENOM; CLU_028888_2_0_1; -.
DR InParanoid; P42292; -.
DR OrthoDB; 536204at2759; -.
DR PhylomeDB; P42292; -.
DR PRO; PR:P42292; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000015348; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; P42292; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:AgBase.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0098743; P:cell aggregation; IDA:AgBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:AgBase.
DR GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
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; IPR003599; Ig_sub.
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; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell adhesion; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:1608932,
FT ECO:0000269|PubMed:1931049"
FT CHAIN 34..588
FT /note="CD166 antigen"
FT /id="PRO_0000014662"
FT TOPO_DOM 34..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..126
FT /note="Ig-like V-type 1"
FT DOMAIN 131..240
FT /note="Ig-like V-type 2"
FT DOMAIN 251..333
FT /note="Ig-like C2-type 1"
FT DOMAIN 338..414
FT /note="Ig-like C2-type 2"
FT DOMAIN 421..501
FT /note="Ig-like C2-type 3"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 163..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 359..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 440..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 1..10
FT /note="MMEPPAAAAR -> MEPPSRRRP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="A -> S (in Ref. 3; AAA48602)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..113
FT /note="SD -> RH (in Ref. 3; AAA48602)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="A -> T (in Ref. 2; CAA45579)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="LQ -> HK (in Ref. 2; CAA45579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 65726 MW; 2A28612D0164531E CRC64;
MMEPPAAAAR ASCRRRPLLC LLLAALCMPP ALGLYTVNAV YGDTITMPCR LEVPDGLMFG
KWKYEMPNGS PVFIAFRSST KKNVQYDDVP DYKDRLSLSE NYTLSIKNAR ISDEKRFVCM
LVTEDDVSEE PTVVKVFKQP SQPEILHQAD FLETEKLKML GECVVRDSYP EGNVTWYKNG
RVLQPVEEVV VINLRKVENR STGLFTMTSS LQYMPTKEDA NAKFTCIVTY HGPSGQKTIQ
SEPVVFDVHY PTEKVTIRVL SQSSTIKEGD NVTLKCSGNG NPPPQEFLFY IPGETEGIRS
SDTYVMTDVR RNATGEYKCS LIDKSMMDAT TITVHYLDLQ LTPSGEVTKQ IGEALPVSCT
ISSSRNATVF WIKDNTRMKT SPSFSSLQYQ DAGNYICETT LQEVEGLKKR KTLKLIVEGK
PQIKMTKKTN TNKMSKTIVC HVEGFPKPAV QWTVTGSGSL INKTEETKYV NGKFSSKIII
APEENVTLTC IAENELERTV TSLNVSAISI PEYDEPEDRN DDNSEKVNDQ AKLIVGIVVG
LLLVALVAGV VYWLYVKKSK TASKHVDKDL GNIEENKKLE ENNHKSET
