CSA_DICDI
ID CSA_DICDI Reviewed; 514 AA.
AC P08796; P19408; Q54I06;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Contact site A protein;
DE Short=CSA;
DE AltName: Full=Cell adhesion molecule gp80;
DE AltName: Full=Membrane-associated glycoprotein gp80;
DE Flags: Precursor;
GN Name=csaA; ORFNames=DDB_G0289073;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16453689; DOI=10.1002/j.1460-2075.1986.tb04384.x;
RA Noegel A., Gerisch G., Stadler J., Westphal M.;
RT "Complete sequence and transcript regulation of a cell adhesion protein
RT from aggregating Dictyostelium cells.";
RL EMBO J. 5:1473-1476(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3063296; DOI=10.1139/o88-126;
RA Siu C.-H., Wong L.M., Lam T.Y., Kamboj R.K., Choi A., Cho A.;
RT "Molecular mechanisms of cell-cell interaction in Dictyostelium
RT discoideum.";
RL Biochem. Cell Biol. 66:1089-1099(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX2;
RX PubMed=1326559; DOI=10.1016/s0021-9258(18)41825-x;
RA Desbarats L., Lam T.Y., Wong L.M., Siu C.-H.;
RT "Identification of a unique cAMP-response element in the gene encoding the
RT cell adhesion molecule gp80 in Dictyostelium discoideum.";
RL J. Biol. Chem. 267:19655-19664(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [5]
RP PROTEIN SEQUENCE OF 20-46.
RX PubMed=7118072; DOI=10.1515/bchm2.1982.363.2.771;
RA Stadler J., Bordier C., Lottspeich F., Henschen A., Gerisch G.;
RT "Improved purification and N-terminal amino acid sequence determination of
RT the contact site A glycoprotein of Dictyostelium discoideum.";
RL Hoppe-Seyler's Z. Physiol. Chem. 363:771-776(1982).
RN [6]
RP PROTEIN SEQUENCE OF 20-49.
RX PubMed=16593709; DOI=10.1073/pnas.83.12.4248;
RA Wong L.M., Siu C.-H.;
RT "Cloning of cDNA for the contact site A glycoprotein of Dictyostelium
RT discoideum.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4248-4252(1986).
RN [7]
RP PROTEIN SEQUENCE OF 132-139.
RX PubMed=2582489; DOI=10.1016/0092-8674(89)90007-x;
RA Kamboj R.K., Gariepy J., Siu C.-H.;
RT "Identification of an octapeptide involved in homophilic interaction of the
RT cell adhesion molecule gp80 of Dictyostelium discoideum.";
RL Cell 59:615-625(1989).
RN [8]
RP CELL-BINDING DOMAIN.
RX PubMed=3182938; DOI=10.1083/jcb.107.5.1835;
RA Kamboj R.K., Wong L.M., Lam T.Y., Siu C.-H.;
RT "Mapping of a cell-binding domain in the cell adhesion molecule gp80 of
RT Dictyostelium discoideum.";
RL J. Cell Biol. 107:1835-1843(1988).
RN [9]
RP GPI-ANCHOR.
RX PubMed=2721485; DOI=10.1002/j.1460-2075.1989.tb03387.x;
RA Stadler J., Keenan T.W., Bauer G., Gerisch G.;
RT "The contact site A glycoprotein of Dictyostelium discoideum carries a
RT phospholipid anchor of a novel type.";
RL EMBO J. 8:371-377(1989).
CC -!- FUNCTION: This cell-surface glycoprotein mediates cell-cell binding via
CC homophilic interaction.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Note=Attached to the membrane by a GPI-anchor that contains a
CC phosphoceramide moiety. Such anchor mediates a fast and long
CC persistence cell adhesion of the protein.
CC -!- DEVELOPMENTAL STAGE: Restricted to the aggregation stage of development
CC of D.discoideum.
CC -!- DOMAIN: The C-terminal region contains clusters of proline regularly
CC alternating with a hydroxyamino acid. This domain might act as a spacer
CC to elevate sites active in cell contact into the extracellular space.
CC -!- PTM: Phosphorylated on serine and N-glycosylated with two types of
CC oligosaccharide chains.
CC -!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather than
CC a phosphatidyl group.
CC -!- MISCELLANEOUS: The expression of this stringently regulated protein
CC during cell development is mediated through cell-surface cAMP
CC receptors.
CC -!- CAUTION: The Dictyosteliida are known to produce a
CC glycosylsphingolipidinositol anchor (GPI-like-anchor). It has not been
CC established whether Dictyosteliida make a glycosylphosphatidylinositol
CC anchor (GPI-anchor) also, and whether their GPI-like-anchor
CC modifications can be interconverted with GPI-anchor modifications in a
CC resculpting process. It has not been established that the GPI-like-
CC anchor modification in Dictyosteliida utilizes the same sequence motif.
CC {ECO:0000305}.
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DR EMBL; X04004; CAA27634.1; -; mRNA.
DR EMBL; M36545; AAA33212.1; -; mRNA.
DR EMBL; X66483; CAA47110.1; -; Genomic_DNA.
DR EMBL; AAFI02000130; EAL62886.1; -; Genomic_DNA.
DR PIR; A44100; A44100.
DR PIR; S22066; A31643.
DR RefSeq; XP_636399.1; XM_631307.1.
DR AlphaFoldDB; P08796; -.
DR STRING; 44689.DDB0191156; -.
DR PaxDb; P08796; -.
DR ABCD; P08796; 2 sequenced antibodies.
DR EnsemblProtists; EAL62886; EAL62886; DDB_G0289073.
DR GeneID; 8626958; -.
DR KEGG; ddi:DDB_G0289073; -.
DR dictyBase; DDB_G0289073; csaA.
DR eggNOG; ENOG502RI6S; Eukaryota.
DR HOGENOM; CLU_530458_0_0_1; -.
DR InParanoid; P08796; -.
DR OMA; NNGRIGM; -.
DR PhylomeDB; P08796; -.
DR PRO; PR:P08796; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0046658; C:anchored component of plasma membrane; TAS:dictyBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0045121; C:membrane raft; TAS:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IMP:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IDA:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; TAS:dictyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:0010225; P:response to UV-C; IDA:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR SUPFAM; SSF81296; SSF81296; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:16593709,
FT ECO:0000269|PubMed:7118072"
FT CHAIN 20..492
FT /note="Contact site A protein"
FT /id="PRO_0000021010"
FT PROPEP 493..514
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021011"
FT DOMAIN 21..104
FT /note="IPT/TIG 1"
FT DOMAIN 191..283
FT /note="IPT/TIG 2"
FT REPEAT 462..469
FT /note="1"
FT REPEAT 472..479
FT /note="2"
FT REGION 20..453
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 446..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..479
FT /note="2 X 8 AA repeats, Pro-rich"
FT COMPBIAS 460..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 492
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 216
FT /note="G -> V (in Ref. 2; AAA33212 and 3; CAA47110)"
FT /evidence="ECO:0000305"
SQ 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
