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Cell-cell adhesion glycoprotein 64 (Gp64) (Contact site 1)

 GP64_POLPA              Reviewed;         320 AA.
Q52085; Q9U8R5;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 49.
RecName: Full=Cell-cell adhesion glycoprotein 64;
Short=Gp64 {ECO:0000303|PubMed:6538484, ECO:0000303|PubMed:8276846, ECO:0000312|EMBL:BAA03637.1};
AltName: Full=Contact site 1 {ECO:0000303|PubMed:7195818};
Flags: Precursor;
Name=gp64 {ECO:0000303|PubMed:8276846};
Synonyms=c-p644 {ECO:0000312|EMBL:BAA03637.1};
Polysphondylium pallidum (Cellular slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Polysphondylium.
NCBI_TaxID=13642;
[1] {ECO:0000305, ECO:0000312|EMBL:BAA03637.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-39 AND 285-298,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
STRAIN=ATCC 44843 / DSM 1394 / WS320 {ECO:0000312|EMBL:BAA03637.1};
PubMed=8276846;
Manabe R., Saito T., Kumazaki T., Sakaitani T., Nakata N., Ochiai H.;
"Molecular cloning and the COOH-terminal processing of gp64, a
putative cell-cell adhesion protein of the cellular slime mold
Polysphondylium pallidum.";
J. Biol. Chem. 269:528-535(1994).
[2] {ECO:0000305, ECO:0000312|EMBL:BAA86631.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 44843 / DSM 1394 / WS320 {ECO:0000312|EMBL:BAA86631.1};
PubMed=10542319; DOI=10.1016/S0167-4781(99)00179-7;
Takaoka N., Fukuzawa M., Saito T., Sakaitani T., Ochiai H.;
"Promoter analysis of the membrane protein gp64 gene of the cellular
slime mold Polysphondylium pallidum.";
Biochim. Biophys. Acta 1447:226-230(1999).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 28-41; 48-53; 78-107; 134-144; 151-162; 181-192;
207-219 AND 285-299, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-49;
ASN-80; ASN-141; ASN-158; ASN-187 AND ASN-216.
PubMed=8425525; DOI=10.1111/j.1432-1033.1993.tb19881.x;
Saito T., Kumazaki T., Ochiai H.;
"A purification method and N-glycosylation sites of a 36-cysteine-
containing, putative cell/cell adhesion glycoprotein gp64 of the
cellular slime mold, Polysphondylium pallidum.";
Eur. J. Biochem. 211:147-155(1993).
[4] {ECO:0000305}
PROTEIN SEQUENCE OF 38-43; 56-58; 63-91; 94-119; 122-124; 130-139;
146-150; 156-179; 184-213; 223-226; 230-249; 264-266; 268-272 AND
280-289, AND DISULFIDE BONDS.
PubMed=7961835;
Saito T., Kumazaki T., Ochiai H.;
"Assignment of disulfide bonds in gp64, a putative cell-cell adhesion
protein of Polysphondylium pallidum. Presence of Sushi domains in the
cellular slime mold protein.";
J. Biol. Chem. 269:28798-28802(1994).
[5] {ECO:0000305}
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
AND GLYCOSYLATION.
PubMed=7195818; DOI=10.1016/0014-4827(81)90475-4;
Bozzaro S., Tsugita A., Janku M., Monok G., Opatz K., Gerisch G.;
"Characterization of a purified cell surface glycoprotein as a contact
site in Polysphondylium pallidum.";
Exp. Cell Res. 134:181-191(1981).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
GLYCOSYLATION.
PubMed=6538484; DOI=10.1111/j.1432-1033.1984.tb08068.x;
Toda K., Bozzaro S., Lottspeich F., Merkl R., Gerisch G.;
"Monoclonal anti-glycoprotein antibody that blocks cell adhesion in
Polysphondylium pallidum.";
Eur. J. Biochem. 140:73-81(1984).
[7] {ECO:0000305}
SUBCELLULAR LOCATION, AND GPI-ANCHOR AT SER-298.
PubMed=8269952; DOI=10.1111/j.1432-1033.1993.tb18415.x;
Saito T., Ochiai H.;
"Evidence for a glycolipid anchor of gp64, a putative cell-cell
adhesion protein of Polysphondylium pallidum.";
Eur. J. Biochem. 218:623-628(1993).
[8] {ECO:0000305}
FUNCTION.
PubMed=8743948;
Funamoto S., Ochiai H.;
"Antisense RNA inactivation of gene expression of a cell-cell adhesion
protein (gp64) in the cellular slime mold Polysphondylium pallidum.";
J. Cell Sci. 109:1009-1016(1996).
-!- FUNCTION: Cell-cell adhesion during development.
{ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
ECO:0000269|PubMed:8276846, ECO:0000269|PubMed:8743948}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6538484,
ECO:0000269|PubMed:7195818, ECO:0000269|PubMed:8269952,
ECO:0000269|PubMed:8276846}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
ECO:0000269|PubMed:8269952, ECO:0000269|PubMed:8276846}.
Note=Attached to the membrane by a GPI-like-anchor that contains a
phosphoceramide group. {ECO:0000269|PubMed:6538484,
ECO:0000269|PubMed:7195818, ECO:0000269|PubMed:8269952,
ECO:0000269|PubMed:8276846}.
-!- DEVELOPMENTAL STAGE: Expressed in vegetative cells and throughout
development. Levels peak during the aggregation stage before
declining and then rising again during culmination (at protein
level). {ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
ECO:0000269|PubMed:8276846}.
-!- PTM: Contains 18 disulfide bonds. {ECO:0000269|PubMed:7961835,
ECO:0000269|PubMed:8425525}.
-!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather
than a phosphatidyl group. {ECO:0000269|PubMed:8269952}.
-!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition)
shows reduced cell adhesiveness and forms smaller aggregates than
wild-type, though it does complete development and produce
fruiting bodies. {ECO:0000269|PubMed:8743948}.
-!- 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), 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 as the GPI-anchor
modification. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D14993; BAA03637.1; -; mRNA.
EMBL; AB027502; BAA86631.1; -; Genomic_DNA.
PIR; A53119; A53119.
ProteinModelPortal; Q52085; -.
iPTMnet; Q52085; -.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Developmental protein;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:8276846}.
CHAIN 20 298 Cell-cell adhesion glycoprotein 64.
/FTId=PRO_0000371261.
PROPEP 299 320 Removed in mature form.
{ECO:0000269|PubMed:8276846}.
/FTId=PRO_0000371262.
LIPID 298 298 GPI-like-anchor amidated serine.
{ECO:0000269|PubMed:8269952}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8425525}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8425525}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8425525}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8425525}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8425525}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8425525}.
DISULFID 39 57 {ECO:0000269|PubMed:7961835}.
DISULFID 67 79 {ECO:0000269|PubMed:7961835}.
DISULFID 73 86 {ECO:0000269|PubMed:7961835}.
DISULFID 98 110 {ECO:0000269|PubMed:7961835}.
DISULFID 104 115 {ECO:0000269|PubMed:7961835}.
DISULFID 123 138 {ECO:0000269|PubMed:7961835}.
DISULFID 132 147 {ECO:0000269|PubMed:7961835}.
DISULFID 157 171 {ECO:0000269|PubMed:7961835}.
DISULFID 165 176 {ECO:0000269|PubMed:7961835}.
DISULFID 188 202 {ECO:0000269|PubMed:7961835}.
DISULFID 194 207 {ECO:0000269|PubMed:7961835}.
DISULFID 226 246 {ECO:0000269|PubMed:7961835}.
DISULFID 232 234 {ECO:0000269|PubMed:7961835}.
DISULFID 266 285 {ECO:0000269|PubMed:7961835}.
DISULFID 270 281 {ECO:0000269|PubMed:7961835}.
SEQUENCE 320 AA; 32724 MW; AFE158C56845EFAD CRC64;
MNKFITLFVL LASVSVAMSA TCLTCVKEGA VCDATANICE EGTVCIKPNS TAANTICFVL
PTLNEDCSGP LACADSYYCN TTSKICVEAY YLGVGESCSS ENQCSTSLVC TGGKCVNEVY
PLCGASNSRV GCKAGEGCAF NGTALVCSPF IANGAACNTS TSGLCHPVSS CSNGVCTAPL
TGALNSNCTS NTDCNIANGL YCSSGKCTAV PEALNNCTTT PTVDNCLGYS ACMCPSNDDT
AKTGSCKDTI EYSDVTSDAY NKYDSCVVSC PAVTIVQKQS CLSKCTNPLA GAANNVCSSA
TTIAFNAFVV FAIVLSVLLF


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