CD166_CANLF
ID CD166_CANLF Reviewed; 521 AA.
AC O46634;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=CD166 antigen;
DE AltName: Full=Activated leukocyte cell adhesion molecule;
DE AltName: Full=SB-10 antigen {ECO:0000303|PubMed:9556065};
DE AltName: CD_antigen=CD166;
DE Flags: Fragment;
GN Name=ALCAM;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mesenchymal cell;
RX PubMed=9556065; DOI=10.1359/jbmr.1998.13.4.655;
RA Bruder S.P., Ricalton N.S., Boynton R.E., Connolly T.J., Jaiswal N.,
RA Zaia J., Barry F.P.;
RT "Mesenchymal stem cell surface antigen SB-10 corresponds to activated
RT leukocyte cell adhesion molecule and is involved in osteogenic
RT differentiation.";
RL J. Bone Miner. Res. 13:655-663(1998).
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 -!- 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; Y13242; CAA73694.1; -; mRNA.
DR AlphaFoldDB; O46634; -.
DR SMR; O46634; -.
DR STRING; 9615.ENSCAFP00000014280; -.
DR PaxDb; O46634; -.
DR PRIDE; O46634; -.
DR eggNOG; ENOG502RMQM; Eukaryota.
DR InParanoid; O46634; -.
DR Proteomes; UP000002254; 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:0005886; C:plasma membrane; IBA:GO_Central.
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 PANTHER; PTHR11973:SF2; PTHR11973:SF2; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR SMART; SM00409; IG; 2.
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; Transmembrane; Transmembrane helix.
FT CHAIN <1..521
FT /note="CD166 antigen"
FT /id="PRO_0000072677"
FT TOPO_DOM <1..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 63..172
FT /note="Ig-like V-type 2"
FT DOMAIN 183..266
FT /note="Ig-like C2-type 1"
FT DOMAIN 271..347
FT /note="Ig-like C2-type 2"
FT DOMAIN 354..439
FT /note="Ig-like C2-type 3"
FT REGION 500..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 208..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 292..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 373..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 521 AA; 58107 MW; A3616E9A2429E7B6 CRC64;
GSPVFIAFRS STKKSVQYDD VPEYEDRLSL SENYTLSISN ARISDEKRFV CMLVTEDNVF
EAPTIVKVFK QPSKPEIVSK APFLETEQLK KLGDCISKDS YPDGNITWYR NGKVLQPLEG
VVVLIFKKQM DPVTQLYTMT SSLEYKATKA DIQMQFTCSV TYYGPSGQKT VQSEQAIFDI
YYPTEQVTIQ VLPSKTAIKE GDIITLKCLG NGNPPPEEFL FYLPGQPEGI RSSNTYTLTD
VRRNATGDYK CSLIDKKSMI ASTAITVHYL DLSLNPSGEV TKQIGDALPV SCTISASRNA
TVVWMKDNIR LRSSPSFSSL QYQDAGNYVC ETALQEVEGL KKRESLTLIV EGKPQIKMTK
KTDPSGLSKT IICHVEGFPK PAIQWTITGS GSVINQTEES PYINGRYYST IINSPEENVT
LTCTAENQLE RTVNSLNVSA ISIPEHDEAD EISDENREQV NHRATLIVGI VLRLLHGALV
AGVVYWLYVK KSKTASKHVN KDLGNLEENK KLEQNNHRTE A
