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Contact site A protein (CSA) (Cell adhesion molecule gp80) (Membrane-associated glycoprotein gp80)

 CSA_DICDI               Reviewed;         514 AA.
P08796; P19408; Q54I06;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 3.
28-FEB-2018, entry version 115.
RecName: Full=Contact site A protein;
Short=CSA;
AltName: Full=Cell adhesion molecule gp80;
AltName: Full=Membrane-associated glycoprotein gp80;
Flags: Precursor;
Name=csaA; ORFNames=DDB_G0289073;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16453689;
Noegel A., Gerisch G., Stadler J., Westphal M.;
"Complete sequence and transcript regulation of a cell adhesion
protein from aggregating Dictyostelium cells.";
EMBO J. 5:1473-1476(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3063296;
Siu C.-H., Wong L.M., Lam T.Y., Kamboj R.K., Choi A., Cho A.;
"Molecular mechanisms of cell-cell interaction in Dictyostelium
discoideum.";
Biochem. Cell Biol. 66:1089-1099(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AX2;
PubMed=1326559;
Desbarats L., Lam T.Y., Wong L.M., Siu C.-H.;
"Identification of a unique cAMP-response element in the gene encoding
the cell adhesion molecule gp80 in Dictyostelium discoideum.";
J. Biol. Chem. 267:19655-19664(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[5]
PROTEIN SEQUENCE OF 20-46.
PubMed=7118072;
Stadler J., Bordier C., Lottspeich F., Henschen A., Gerisch G.;
"Improved purification and N-terminal amino acid sequence
determination of the contact site A glycoprotein of Dictyostelium
discoideum.";
Hoppe-Seyler's Z. Physiol. Chem. 363:771-776(1982).
[6]
PROTEIN SEQUENCE OF 20-49.
PubMed=16593709; DOI=10.1073/pnas.83.12.4248;
Wong L.M., Siu C.-H.;
"Cloning of cDNA for the contact site A glycoprotein of Dictyostelium
discoideum.";
Proc. Natl. Acad. Sci. U.S.A. 83:4248-4252(1986).
[7]
PROTEIN SEQUENCE OF 132-139.
PubMed=2582489; DOI=10.1016/0092-8674(89)90007-X;
Kamboj R.K., Gariepy J., Siu C.-H.;
"Identification of an octapeptide involved in homophilic interaction
of the cell adhesion molecule gp80 of Dictyostelium discoideum.";
Cell 59:615-625(1989).
[8]
CELL-BINDING DOMAIN.
PubMed=3182938; DOI=10.1083/jcb.107.5.1835;
Kamboj R.K., Wong L.M., Lam T.Y., Siu C.-H.;
"Mapping of a cell-binding domain in the cell adhesion molecule gp80
of Dictyostelium discoideum.";
J. Cell Biol. 107:1835-1843(1988).
[9]
GPI-ANCHOR.
PubMed=2721485;
Stadler J., Keenan T.W., Bauer G., Gerisch G.;
"The contact site A glycoprotein of Dictyostelium discoideum carries a
phospholipid anchor of a novel type.";
EMBO J. 8:371-377(1989).
-!- FUNCTION: This cell-surface glycoprotein mediates cell-cell
binding via homophilic interaction.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Note=Attached to the membrane by a GPI-anchor that contains a
phosphoceramide moiety. Such anchor mediates a fast and long
persistence cell adhesion of the protein.
-!- DEVELOPMENTAL STAGE: Restricted to the aggregation stage of
development of D.discoideum.
-!- DOMAIN: The C-terminal region contains clusters of proline
regularly alternating with a hydroxyamino acid. This domain might
act as a spacer to elevate sites active in cell contact into the
extracellular space.
-!- PTM: Phosphorylated on serine and N-glycosylated with two types of
oligosaccharide chains.
-!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather
than a phosphatidyl group.
-!- MISCELLANEOUS: The expression of this stringently regulated
protein during cell development is mediated through cell-surface
cAMP receptors.
-!- CAUTION: The Dictyosteliida are known to produce a
glycosylsphingolipidinositol anchor (GPI-like-anchor). It has not
been established whether Dictyosteliida make a
glycosylphosphatidylinositol anchor (GPI-anchor) also, and whether
their GPI-like-anchor modifications can be interconverted with
GPI-anchor modifications in a resculpting process. It has not been
established that the GPI-like-anchor modification in
Dictyosteliida utilizes the same sequence motif. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X04004; CAA27634.1; -; mRNA.
EMBL; M36545; AAA33212.1; -; mRNA.
EMBL; X66483; CAA47110.1; -; Genomic_DNA.
EMBL; AAFI02000130; EAL62886.1; -; Genomic_DNA.
PIR; A44100; A44100.
PIR; S22066; A31643.
RefSeq; XP_636399.1; XM_631307.1.
STRING; 44689.DDB0191156; -.
PaxDb; P08796; -.
EnsemblProtists; EAL62886; EAL62886; DDB_G0289073.
GeneID; 8626958; -.
KEGG; ddi:DDB_G0289073; -.
dictyBase; DDB_G0289073; csaA.
InParanoid; P08796; -.
OMA; YESSNTI; -.
PhylomeDB; P08796; -.
PRO; PR:P08796; -.
Proteomes; UP000002195; Chromosome 5.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0044291; C:cell-cell contact zone; IDA:dictyBase.
GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
GO; GO:0030175; C:filopodium; IDA:dictyBase.
GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
GO; GO:0098632; F:cell-cell adhesion mediator activity; IDA:dictyBase.
GO; GO:0042802; F:identical protein binding; IDA:dictyBase.
GO; GO:0042803; F:protein homodimerization activity; TAS:dictyBase.
GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IMP:dictyBase.
GO; GO:0098609; P:cell-cell adhesion; IMP:dictyBase.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IDA:dictyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; TAS:dictyBase.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:dictyBase.
GO; GO:0051260; P:protein homooligomerization; IDA:dictyBase.
GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
SUPFAM; SSF81296; SSF81296; 2.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Glycoprotein; GPI-anchor; Lipoprotein;
Membrane; Phosphoprotein; Reference proteome; Repeat; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:16593709,
ECO:0000269|PubMed:7118072}.
CHAIN 20 492 Contact site A protein.
/FTId=PRO_0000021010.
PROPEP 493 514 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000021011.
DOMAIN 21 104 IPT/TIG 1.
DOMAIN 191 283 IPT/TIG 2.
REPEAT 462 469 1.
REPEAT 472 479 2.
REGION 20 453 Globular. {ECO:0000255}.
REGION 462 479 2 X 8 AA repeats, Pro-rich.
COMPBIAS 454 485 Pro-rich (hinge).
LIPID 492 492 GPI-like-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 216 216 G -> V (in Ref. 2; AAA33212 and 3;
CAA47110). {ECO:0000305}.
SEQUENCE 514 AA; 53655 MW; DB1BA39B56AAD878 CRC64;
MKFLLVLIIL YNILNSAHSA PTITAVSNGK FGVPTYITIT GTGFTGTPVV TIGGQTCDPV
IVANTASLQC QFSAQLAPGN SNFDVIVKVG GVPSTGGNGL FKYTPPTLST IFPNNGRIGM
ILVDGPSNIS GYKLNVNDSI NSAMLSVTAD SVSPTIYFLV PNTIAGGLLN LELIQPFGFS
TIVTSKSVFS PTITSITPLA FDLTPTNVTV TGKYFGTTAS VTMGSHIYTG LTVQDDGTNC
HVIFTTRSVY ESSNTITAKA STGVDMIYLD NQGNQQPITF TYNPPTITST KQVNDSVEIS
TTNTGTDFTQ ISLTMGTSSP TNLVITGTNE KIVITLPHAL PEGEIQFNLK AGISNVVTST
LLVTPVINSV TQAPHNGGSI TISGIFLNNA HVSIVVDQNT TDIVCAPDSN GESIICPVEA
GSGTINLVVT NYKNFASDPT IKTEATTSTT YTIPDTPTPT DTATPSPTPT ETATPSPTPK
PTSTPEETEA PSSATTLISP LSLIVIFISF VLLI


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