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CD166 antigen (Activated leukocyte cell adhesion molecule) (SB-10 antigen) (CD antigen CD166) (Fragment)

 CD166_CANLF             Reviewed;         521 AA.
O46634;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
28-FEB-2018, entry version 88.
RecName: Full=CD166 antigen;
AltName: Full=Activated leukocyte cell adhesion molecule;
AltName: Full=SB-10 antigen {ECO:0000303|PubMed:9556065};
AltName: CD_antigen=CD166;
Flags: Fragment;
Name=ALCAM;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mesenchymal cell;
PubMed=9556065; DOI=10.1359/jbmr.1998.13.4.655;
Bruder S.P., Ricalton N.S., Boynton R.E., Connolly T.J., Jaiswal N.,
Zaia J., Barry F.P.;
"Mesenchymal stem cell surface antigen SB-10 corresponds to activated
leukocyte cell adhesion molecule and is involved in osteogenic
differentiation.";
J. Bone Miner. Res. 13:655-663(1998).
-!- FUNCTION: Cell adhesion molecule that mediates both heterotypic
cell-cell contacts via its interaction with CD6, as well as
homotypic cell-cell contacts. Promotes T-cell activation and
proliferation via its interactions with CD6 (By similarity).
Contributes to the formation and maturation of the immunological
synapse via its interactions with CD6 (By similarity). Mediates
homotypic interactions with cells that express ALCAM. Mediates
attachment of dendritic cells onto endothelial cells via homotypic
interaction. Inhibits endothelial cell migration and promotes
endothelial tube formation via homotypic interactions. Required
for normal organization of the lymph vessel network. Required for
normal hematopoietic stem cell engraftment in the bone marrow.
Plays a role in hematopoiesis; required for normal numbers of
hematopoietic stem cells in bone marrow. Promotes in vitro
osteoblast proliferation and differentiation (By similarity).
Promotes neurite extension, axon growth and axon guidance; axons
grow preferentially on surfaces that contain ALCAM (By
similarity). Mediates outgrowth and pathfinding for retinal
ganglion cell axons (By similarity).
{ECO:0000250|UniProtKB:P42292, ECO:0000250|UniProtKB:Q13740,
ECO:0000250|UniProtKB:Q61490}.
-!- SUBUNIT: Homodimer. Interacts (via extracellular domain) with CD6
(via extracellular domain). Homodimerization and interaction with
CD6 involve the same region and cannot occur simultaneously. The
affinity for CD6 is much higher than the affinity for self-
association. Interacts (via glycosylated extracellular domain)
with LGALS1 and LGALS3. Interaction with LGALS1 or LGALS3 inhibits
interaction with CD6. {ECO:0000250|UniProtKB:Q13740}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q61490}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q61490}. Cell projection, axon
{ECO:0000250|UniProtKB:Q61490}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q61490}. Note=Detected at the immunological
synapse, i.e, at the contact zone between antigen-presenting
dendritic cells and T-cells. Colocalizes with CD6 and the TCR/CD3
complex at the immunological synapse.
{ECO:0000250|UniProtKB:Q13740}.
-!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like
domain. {ECO:0000250|UniProtKB:Q13740}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}.
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EMBL; Y13242; CAA73694.1; -; mRNA.
UniGene; Cfa.3742; -.
ProteinModelPortal; O46634; -.
SMR; O46634; -.
STRING; 9615.ENSCAFP00000014280; -.
PaxDb; O46634; -.
eggNOG; ENOG410IFQ2; Eukaryota.
eggNOG; ENOG410ZWU9; LUCA.
HOGENOM; HOG000070101; -.
HOVERGEN; HBG050847; -.
InParanoid; O46634; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0048846; P:axon extension involved in axon guidance; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF08205; C2-set_2; 1.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 4.
2: Evidence at transcript level;
Adaptive immunity; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Reference proteome; Repeat;
Transmembrane; Transmembrane helix.
CHAIN <1 521 CD166 antigen.
/FTId=PRO_0000072677.
TOPO_DOM <1 465 Extracellular. {ECO:0000255}.
TRANSMEM 466 487 Helical. {ECO:0000255}.
TOPO_DOM 488 521 Cytoplasmic. {ECO:0000255}.
DOMAIN 63 172 Ig-like V-type 2.
DOMAIN 183 266 Ig-like C2-type 1.
DOMAIN 271 347 Ig-like C2-type 2.
DOMAIN 354 439 Ig-like C2-type 3.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 95 158 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 208 251 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 292 330 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 373 423 {ECO:0000255|PROSITE-ProRule:PRU00114}.
NON_TER 1 1
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


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