GP64_HETPA
ID GP64_HETPA Reviewed; 320 AA.
AC Q52085; Q9U8R5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Cell-cell adhesion glycoprotein 64;
DE Short=Gp64 {ECO:0000303|PubMed:6538484, ECO:0000303|PubMed:8276846, ECO:0000312|EMBL:BAA03637.1};
DE AltName: Full=Contact site 1 {ECO:0000303|PubMed:7195818};
DE Flags: Precursor;
GN Name=gp64 {ECO:0000303|PubMed:8276846};
GN Synonyms=c-p644 {ECO:0000312|EMBL:BAA03637.1};
OS Heterostelium pallidum (Cellular slime mold) (Polysphondylium pallidum).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC Acytosteliaceae; Heterostelium.
OX NCBI_TaxID=13642;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA03637.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-39 AND 285-298,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=ATCC 44843 / DSM 1394 / WS320 {ECO:0000312|EMBL:BAA03637.1};
RX PubMed=8276846; DOI=10.1016/s0021-9258(17)42381-7;
RA Manabe R., Saito T., Kumazaki T., Sakaitani T., Nakata N., Ochiai H.;
RT "Molecular cloning and the COOH-terminal processing of gp64, a putative
RT cell-cell adhesion protein of the cellular slime mold Polysphondylium
RT pallidum.";
RL J. Biol. Chem. 269:528-535(1994).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA86631.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44843 / DSM 1394 / WS320 {ECO:0000312|EMBL:BAA86631.1};
RX PubMed=10542319; DOI=10.1016/s0167-4781(99)00179-7;
RA Takaoka N., Fukuzawa M., Saito T., Sakaitani T., Ochiai H.;
RT "Promoter analysis of the membrane protein gp64 gene of the cellular slime
RT mold Polysphondylium pallidum.";
RL Biochim. Biophys. Acta 1447:226-230(1999).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 28-41; 48-53; 78-107; 134-144; 151-162; 181-192;
RP 207-219 AND 285-299, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-49; ASN-80;
RP ASN-141; ASN-158; ASN-187 AND ASN-216.
RX PubMed=8425525; DOI=10.1111/j.1432-1033.1993.tb19881.x;
RA Saito T., Kumazaki T., Ochiai H.;
RT "A purification method and N-glycosylation sites of a 36-cysteine-
RT containing, putative cell/cell adhesion glycoprotein gp64 of the cellular
RT slime mold, Polysphondylium pallidum.";
RL Eur. J. Biochem. 211:147-155(1993).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 38-43; 56-58; 63-91; 94-119; 122-124; 130-139; 146-150;
RP 156-179; 184-213; 223-226; 230-249; 264-266; 268-272 AND 280-289, AND
RP DISULFIDE BONDS.
RX PubMed=7961835; DOI=10.1016/s0021-9258(19)61976-9;
RA Saito T., Kumazaki T., Ochiai H.;
RT "Assignment of disulfide bonds in gp64, a putative cell-cell adhesion
RT protein of Polysphondylium pallidum. Presence of Sushi domains in the
RT cellular slime mold protein.";
RL J. Biol. Chem. 269:28798-28802(1994).
RN [5] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RX PubMed=7195818; DOI=10.1016/0014-4827(81)90475-4;
RA Bozzaro S., Tsugita A., Janku M., Monok G., Opatz K., Gerisch G.;
RT "Characterization of a purified cell surface glycoprotein as a contact site
RT in Polysphondylium pallidum.";
RL Exp. Cell Res. 134:181-191(1981).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=6538484; DOI=10.1111/j.1432-1033.1984.tb08068.x;
RA Toda K., Bozzaro S., Lottspeich F., Merkl R., Gerisch G.;
RT "Monoclonal anti-glycoprotein antibody that blocks cell adhesion in
RT Polysphondylium pallidum.";
RL Eur. J. Biochem. 140:73-81(1984).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND GPI-ANCHOR AT SER-298.
RX PubMed=8269952; DOI=10.1111/j.1432-1033.1993.tb18415.x;
RA Saito T., Ochiai H.;
RT "Evidence for a glycolipid anchor of gp64, a putative cell-cell adhesion
RT protein of Polysphondylium pallidum.";
RL Eur. J. Biochem. 218:623-628(1993).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=8743948; DOI=10.1242/jcs.109.5.1009;
RA Funamoto S., Ochiai H.;
RT "Antisense RNA inactivation of gene expression of a cell-cell adhesion
RT protein (gp64) in the cellular slime mold Polysphondylium pallidum.";
RL J. Cell Sci. 109:1009-1016(1996).
CC -!- FUNCTION: Cell-cell adhesion during development.
CC {ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
CC ECO:0000269|PubMed:8276846, ECO:0000269|PubMed:8743948}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6538484,
CC ECO:0000269|PubMed:7195818, ECO:0000269|PubMed:8269952,
CC ECO:0000269|PubMed:8276846}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
CC ECO:0000269|PubMed:8269952, ECO:0000269|PubMed:8276846}. Note=Attached
CC to the membrane by a GPI-like-anchor that contains a phosphoceramide
CC group. {ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
CC ECO:0000269|PubMed:8269952, ECO:0000269|PubMed:8276846}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells and throughout
CC development. Levels peak during the aggregation stage before declining
CC and then rising again during culmination (at protein level).
CC {ECO:0000269|PubMed:6538484, ECO:0000269|PubMed:7195818,
CC ECO:0000269|PubMed:8276846}.
CC -!- PTM: Contains 18 disulfide bonds. {ECO:0000269|PubMed:7961835,
CC ECO:0000269|PubMed:8425525}.
CC -!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather than
CC a phosphatidyl group. {ECO:0000269|PubMed:8269952}.
CC -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) shows
CC reduced cell adhesiveness and forms smaller aggregates than wild-type,
CC though it does complete development and produce fruiting bodies.
CC {ECO:0000269|PubMed:8743948}.
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), and whether their GPI-like-anchor modifications
CC can be interconverted with GPI-anchor modifications in a 'resculpting
CC process'. It has not been established that the GPI-like-anchor
CC modification in Dictyosteliida utilizes the same sequence motif as the
CC GPI-anchor modification. {ECO:0000305}.
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DR EMBL; D14993; BAA03637.1; -; mRNA.
DR EMBL; AB027502; BAA86631.1; -; Genomic_DNA.
DR PIR; A53119; A53119.
DR AlphaFoldDB; Q52085; -.
DR iPTMnet; Q52085; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Developmental protein;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8276846"
FT CHAIN 20..298
FT /note="Cell-cell adhesion glycoprotein 64"
FT /id="PRO_0000371261"
FT PROPEP 299..320
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:8276846"
FT /id="PRO_0000371262"
FT LIPID 298
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:8269952"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8425525"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8425525"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8425525"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8425525"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8425525"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8425525"
FT DISULFID 39..57
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 67..79
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 73..86
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 98..110
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 104..115
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 123..138
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 132..147
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 157..171
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 165..176
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 188..202
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 194..207
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 226..246
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 232..234
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 266..285
FT /evidence="ECO:0000269|PubMed:7961835"
FT DISULFID 270..281
FT /evidence="ECO:0000269|PubMed:7961835"
SQ 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
