Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CD166 antigen

Gene

ALCAM

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (PubMed:1931049, PubMed:22421359). 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 (PubMed:1873027, PubMed:22421359). Mediates outgrowth and pathfinding for retinal ganglion cell axons (PubMed:22421359).By similarity3 Publications

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • axon extension involved in axon guidance Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • motor neuron axon guidance Source: Ensembl
  • neuron projection extension Source: UniProtKB
  • retinal ganglion cell axon guidance Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Cell adhesion, Immunity

Names & Taxonomyi

Protein namesi
Recommended name:
CD166 antigen
Alternative name(s):
Activated leukocyte cell adhesion molecule
BEN glycoprotein2 Publications
Protein DM-GRASP1 Publication
Protein JC7
SC1 glycoprotein
CD_antigen: CD166
Gene namesi
Name:ALCAM
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 1

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 532499ExtracellularSequence analysisAdd
BLAST
Transmembranei533 – 55321HelicalSequence analysisAdd
BLAST
Topological domaini554 – 58835CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33332 PublicationsAdd
BLAST
Chaini34 – 588555CD166 antigenPRO_0000014662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 119PROSITE-ProRule annotation
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence analysis
Disulfide bondi163 ↔ 226PROSITE-ProRule annotation
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence analysis
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence analysis
Disulfide bondi276 ↔ 319PROSITE-ProRule annotation
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi359 ↔ 397PROSITE-ProRule annotation
Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi440 ↔ 490PROSITE-ProRule annotation
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence analysis
Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence analysis
Glycosylationi504 – 5041N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP42292.
PRIDEiP42292.

Expressioni

Tissue specificityi

Detected in embryo (PubMed:1931049, PubMed:1608932). Detected in embryonic spinal cord and embryonic brain (PubMed:1873027, PubMed:1313497). Within the spinal cord it is localized to axons in the dorsal funiculus, midline floor plate cells, and motoneurons (PubMed:1873027). Detected in embryonic epithelia and brain (PubMed:1608932). After hatching, detected in bursa of Fabricius and thymus (PubMed:1608932). Detected on embryonic retinal ganglion cell axon growth cones (at protein level) (PubMed:22421359). Detected in embryonic retina and in the optic fiber layer, which is composed of retinal ganglion cell axons and their growth cones (PubMed:22421359).5 Publications

Developmental stagei

Widely expressed during embryonic development.2 Publications

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000024723.

Structurei

3D structure databases

ProteinModelPortaliP42292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 12693Ig-like V-type 1Add
BLAST
Domaini131 – 240110Ig-like V-type 2Add
BLAST
Domaini251 – 33383Ig-like C2-type 1Add
BLAST
Domaini338 – 41477Ig-like C2-type 2Add
BLAST
Domaini421 – 50181Ig-like C2-type 3Add
BLAST

Domaini

The CD6 binding site is located in the N-terminal Ig-like domain.By similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFQ2. Eukaryota.
ENOG410ZWU9. LUCA.
GeneTreeiENSGT00530000063457.
HOGENOMiHOG000070101.
HOVERGENiHBG050847.
InParanoidiP42292.
KOiK06547.
OMAiIQWTITG.
PhylomeDBiP42292.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00406. IGv. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42292-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMEPPAAAAR ASCRRRPLLC LLLAALCMPP ALGLYTVNAV YGDTITMPCR
60 70 80 90 100
LEVPDGLMFG KWKYEMPNGS PVFIAFRSST KKNVQYDDVP DYKDRLSLSE
110 120 130 140 150
NYTLSIKNAR ISDEKRFVCM LVTEDDVSEE PTVVKVFKQP SQPEILHQAD
160 170 180 190 200
FLETEKLKML GECVVRDSYP EGNVTWYKNG RVLQPVEEVV VINLRKVENR
210 220 230 240 250
STGLFTMTSS LQYMPTKEDA NAKFTCIVTY HGPSGQKTIQ SEPVVFDVHY
260 270 280 290 300
PTEKVTIRVL SQSSTIKEGD NVTLKCSGNG NPPPQEFLFY IPGETEGIRS
310 320 330 340 350
SDTYVMTDVR RNATGEYKCS LIDKSMMDAT TITVHYLDLQ LTPSGEVTKQ
360 370 380 390 400
IGEALPVSCT ISSSRNATVF WIKDNTRMKT SPSFSSLQYQ DAGNYICETT
410 420 430 440 450
LQEVEGLKKR KTLKLIVEGK PQIKMTKKTN TNKMSKTIVC HVEGFPKPAV
460 470 480 490 500
QWTVTGSGSL INKTEETKYV NGKFSSKIII APEENVTLTC IAENELERTV
510 520 530 540 550
TSLNVSAISI PEYDEPEDRN DDNSEKVNDQ AKLIVGIVVG LLLVALVAGV
560 570 580
VYWLYVKKSK TASKHVDKDL GNIEENKKLE ENNHKSET
Length:588
Mass (Da):65,726
Last modified:November 1, 1995 - v1
Checksum:i2A28612D0164531E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1010MMEPPAAAAR → MEPPSRRRP AA sequence (PubMed:1608932).Curated
Sequence conflicti25 – 251A → S in AAA48602 (PubMed:1608932).Curated
Sequence conflicti112 – 1132SD → RH in AAA48602 (PubMed:1608932).Curated
Sequence conflicti329 – 3291A → T in CAA45579 (PubMed:1873027).Curated
Sequence conflicti401 – 4022LQ → HK in CAA45579 (PubMed:1873027).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S63276 mRNA. Translation: AAB20170.1.
M76678 mRNA. Translation: AAA48602.1.
X64301 mRNA. Translation: CAA45579.1.
PIRiA45254.
JH0464.
JH0506.
RefSeqiNP_990510.1. NM_205179.1.
UniGeneiGga.2734.

Genome annotation databases

EnsembliENSGALT00000024769; ENSGALP00000024723; ENSGALG00000015348.
GeneIDi396092.
KEGGigga:396092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S63276 mRNA. Translation: AAB20170.1.
M76678 mRNA. Translation: AAA48602.1.
X64301 mRNA. Translation: CAA45579.1.
PIRiA45254.
JH0464.
JH0506.
RefSeqiNP_990510.1. NM_205179.1.
UniGeneiGga.2734.

3D structure databases

ProteinModelPortaliP42292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000024723.

Proteomic databases

PaxDbiP42292.
PRIDEiP42292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000024769; ENSGALP00000024723; ENSGALG00000015348.
GeneIDi396092.
KEGGigga:396092.

Organism-specific databases

CTDi214.

Phylogenomic databases

eggNOGiENOG410IFQ2. Eukaryota.
ENOG410ZWU9. LUCA.
GeneTreeiENSGT00530000063457.
HOGENOMiHOG000070101.
HOVERGENiHBG050847.
InParanoidiP42292.
KOiK06547.
OMAiIQWTITG.
PhylomeDBiP42292.

Miscellaneous databases

NextBioi20816150.
PROiP42292.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00406. IGv. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of a novel adhesion molecule, SC1."
    Tanaka H., Matsui T., Agata A., Tomura M., Kubota I., McFarland K.C., Kohr B., Lee A., Phillips H.S., Shelton D.L.
    Neuron 7:535-545(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF 34-53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "DM-GRASP, a novel immunoglobulin superfamily axonal surface protein that supports neurite extension."
    Burns F.R., von Kannen S., Guy L., Raper J.A., Kamholz J., Chang S.
    Neuron 7:209-220(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
  3. "BEN, a surface glycoprotein of the immunoglobulin superfamily, is expressed in a variety of developing systems."
    Pourquie O., Corbel C., Le Caer J.-P., Rossier J., le Douarin N.M.
    Proc. Natl. Acad. Sci. U.S.A. 89:5261-5265(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-52; 87-93; 504-512 AND 569-582, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    Tissue: Bursa of Fabricius.
  4. "Association of BEN glycoprotein expression with climbing fiber axonogenesis in the avian cerebellum."
    Pourquie O., Hallonet M.E.R., le Douarin N.M.
    J. Neurosci. 12:1548-1557(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION, TISSUE SPECIFICITY.
  5. "Translation of the cell adhesion molecule ALCAM in axonal growth cones - regulation and functional importance."
    Thelen K., Maier B., Faber M., Albrecht C., Fischer P., Pollerberg G.E.
    J. Cell Sci. 125:1003-1014(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCD166_CHICK
AccessioniPrimary (citable) accession number: P42292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.