CD166_BOVIN
ID CD166_BOVIN Reviewed; 583 AA.
AC Q9BH13;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=CD166 antigen;
DE AltName: Full=Activated leukocyte cell adhesion molecule;
DE AltName: CD_antigen=CD166;
DE Flags: Precursor;
GN Name=ALCAM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Holstein-Friesian; TISSUE=Cervicothoracic ganglion;
RX PubMed=11404380;
RA Konno A., Ahn J.-S., Kitamura H., Hamilton M.J., Gebe J.A., Aruffo A.,
RA Davis W.C.;
RT "Tissue distribution of CD6 and CD6 ligand in cattle: expression of the CD6
RT ligand (CD166) in the autonomic nervous system of cattle and the human.";
RL J. Leukoc. Biol. 69:944-950(2001).
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 Interacts (via glycosylated extracellular domain) with LGALS1 and
CC LGALS3. Interaction with LGALS1 or LGALS3 inhibits interaction with
CC CD6. {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: Constitutively expressed in the autonomic nervous
CC system. Sympathetic and parasympathetic nerve fibers but not myelinated
CC nerve fibers in the spinal nerve. {ECO:0000269|PubMed:11404380}.
CC -!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like
CC domain. {ECO:0000250|UniProtKB:Q13740}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}.
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DR EMBL; AB039957; BAB32790.1; -; mRNA.
DR RefSeq; NP_776663.1; NM_174238.1.
DR AlphaFoldDB; Q9BH13; -.
DR SMR; Q9BH13; -.
DR STRING; 9913.ENSBTAP00000000097; -.
DR PaxDb; Q9BH13; -.
DR PeptideAtlas; Q9BH13; -.
DR PRIDE; Q9BH13; -.
DR GeneID; 281614; -.
DR KEGG; bta:281614; -.
DR CTD; 214; -.
DR eggNOG; ENOG502RMQM; Eukaryota.
DR InParanoid; Q9BH13; -.
DR OrthoDB; 536204at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; ISS: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; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS: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; IPR003598; Ig_sub2.
DR PANTHER; PTHR11973:SF2; PTHR11973:SF2; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..583
FT /note="CD166 antigen"
FT /id="PRO_0000014658"
FT TOPO_DOM 28..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..120
FT /note="Ig-like V-type 1"
FT DOMAIN 125..234
FT /note="Ig-like V-type 2"
FT DOMAIN 245..328
FT /note="Ig-like C2-type 1"
FT DOMAIN 333..409
FT /note="Ig-like C2-type 2"
FT DOMAIN 416..501
FT /note="Ig-like C2-type 3"
FT REGION 562..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 354..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 435..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 583 AA; 64766 MW; 56B69D0C135B5BA5 CRC64;
MASKAAPSCR LVFCLLISAT VLRPGLGWYT VNSAYGDTII MPCRVDVPQN LMFGKWKYEK
PDGSPVFIAF RSSTKKSVQY DDVPEYKDRL NLSENYTLSI SNAKISDEKR FVCMLVTEDD
VFEAPTVVKV FKQPSKPEIV SKAPFLETDK LKKLGECISK DSYPDGNITW YRNGKVLQAL
EGAVVIIFRK QMDSVTQLYT MTSSLEYKTT KADIQMPFTC SVTYYGPSGQ KTVYSEQAVF
DIYYPTEQVT IQVLPSKNAI KEGDNITLKC LGNGNPPPEE FLFYLPGQPE GIRSSNTYTL
TDVKRNATGD YKCSLVDKKS MIASAAITVH YLDLSLNPSG EVTKQIGDAL PVSCTISASR
NATVVWMKDN VKLRSSPSFS SLHYQDAGNY VCETALQEVE GLKKRESLTL IVEGKPQIKM
TKKTDPSGLS KTIICHVEGF PKPAIQWTIT GSGSVINQTE ESPYINGRYY SKIIISPEEN
VTLTCTAENQ LERTVNSLNV SAISIPEHDE ADEISDENKE KVNDQAKLIV GIVVGLLLAA
LVAGVVYWLY MKKSKTASKH VNKDLGNMEE NKKLEENNHK TEA
