CD166_RAT
ID CD166_RAT Reviewed; 583 AA.
AC O35112; O55172;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=CD166 antigen;
DE AltName: Full=Activated leukocyte cell adhesion molecule;
DE AltName: Full=HB2 {ECO:0000303|PubMed:9201982};
DE AltName: Full=KG-CAM {ECO:0000303|PubMed:8004458};
DE AltName: Full=Protein MEMD;
DE AltName: Full=SB-10 antigen {ECO:0000303|PubMed:9556065};
DE AltName: CD_antigen=CD166;
DE Flags: Precursor;
GN Name=Alcam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9201982; DOI=10.1074/jbc.272.27.16778;
RA Matsumoto A., Mitchell A., Kurata H., Pyle L., Kondo K., Itakura H.,
RA Fidge N.;
RT "Cloning and characterization of HB2, a candidate high density lipoprotein
RT receptor. Sequence homology with members of the immunoglobulin superfamily
RT of membrane proteins.";
RL J. Biol. Chem. 272:16778-16782(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 29-38.
RX PubMed=8004458; DOI=10.1016/0006-8993(94)91885-6;
RA Peduzzi J.D., Irwin M.H., Geisert E.E. Jr.;
RT "Distribution and characteristics of a 90 kDa protein, KG-CAM, in the rat
RT CNS.";
RL Brain Res. 640:296-307(1994).
RN [4]
RP PROTEIN SEQUENCE OF 45-55; 58-71; 77-87; 111-129; 143-152; 154-160;
RP 176-189; 306-312 AND 406-423, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-156 AND 270-361.
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).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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: Strongest expression in the lung, then brain,
CC liver, and kidney. Present in the somatosensory system, basal ganglia,
CC cortex, olfactory system, and circumventricular organs.
CC -!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like
CC domain. {ECO:0000250|UniProtKB:Q13740}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB008538; BAA23279.1; -; mRNA.
DR EMBL; BC061970; AAH61970.1; -; mRNA.
DR EMBL; Y13240; CAA73692.1; -; mRNA.
DR EMBL; Y13241; CAA73693.1; -; mRNA.
DR RefSeq; NP_113941.1; NM_031753.1.
DR AlphaFoldDB; O35112; -.
DR SMR; O35112; -.
DR STRING; 10116.ENSRNOP00000002738; -.
DR GlyGen; O35112; 8 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; O35112; -.
DR SwissPalm; O35112; -.
DR PaxDb; O35112; -.
DR PRIDE; O35112; -.
DR GeneID; 79559; -.
DR KEGG; rno:79559; -.
DR UCSC; RGD:619972; rat.
DR CTD; 214; -.
DR RGD; 619972; Alcam.
DR VEuPathDB; HostDB:ENSRNOG00000001989; -.
DR eggNOG; ENOG502RMQM; Eukaryota.
DR HOGENOM; CLU_028888_2_0_1; -.
DR InParanoid; O35112; -.
DR OMA; GIVYWLY; -.
DR OrthoDB; 536204at2759; -.
DR PhylomeDB; O35112; -.
DR TreeFam; TF321859; -.
DR PRO; PR:O35112; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001989; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; O35112; RN.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
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:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0007411; P:axon guidance; ISO:RGD.
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:0008045; P:motor neuron axon guidance; ISO:RGD.
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; 3.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..583
FT /note="CD166 antigen"
FT /id="PRO_0000014661"
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 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
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"
FT CONFLICT 339
FT /note="S -> G (in Ref. 5; CAA73693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 65022 MW; D36B73854F5DF61E CRC64;
MASKGSPSCR LVFCLLISAA VLRPGLGWYT VNSAYGDTIV MPCRLDVPQN LMFGKWKYEK
PDGSPVFIAF RSSTKKSVQY DDVPEYKDRL SLSENYTLSI NNAKISDEKR FVCMLVTEDN
VFEAPTLVKV FKQPSKPEIV NRAAFLETEQ LKKLGDCISR DSYPDGNITW YRNGKVLQPV
DGEVSILFKK EIDPGTQLYT MTSSLEYKTT KSDIQMPFTC SVTYYGPSGQ KTIYSEQAIF
DIYYPTEQVT IQVLPPKNAI KEGDNITLQC LGNGNPPPEE FMFYLPGQAE GIRSSNTYTL
TDVRRNATGD YKCSLIDQRN MAASTTITVH YLDLSLNPSG EVTKQIGDTL PVSCTISASR
NATVVWMKDN IRLRSSPSFS SLHYQDAGNY VCETALQEVE GLKKRESLTL IVEGKPQIKM
TKKTDPSGLS KTIICHVEGF PKPAIQWTIT GSGSVINQTE ESPYINGRYY SKIIISPEEN
VTLTCTAENQ LERTVNSLNV SAISIPEHDE ADDISDENRE KVNDQAKLIV GIVVGLLLAA
LVAGVVYWLY MKKSKTASKH VNKDLGNMEE NKKLEENNHK TEA
