PHG1A_DICDI
ID PHG1A_DICDI Reviewed; 641 AA.
AC Q55FP0; Q95ZG2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Putative phagocytic receptor 1a;
DE Flags: Precursor;
GN Name=phg1a; Synonyms=phg1; ORFNames=DDB_G0267444;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AX3 / DH1;
RX PubMed=10944536; DOI=10.1074/jbc.m006725200;
RA Cornillon S., Pech E., Benghezal M., Ravanel K., Gaynor E., Letourneur F.,
RA Bruckert F., Cosson P.;
RT "Phg1p is a nine-transmembrane protein superfamily member involved in
RT dictyostelium adhesion and phagocytosis.";
RL J. Biol. Chem. 275:34287-34292(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=AX3 / DH1;
RX PubMed=12857872; DOI=10.1091/mbc.e02-11-0724;
RA Benghezal M., Cornillon S., Gebbie L., Alibaud L., Bruckert F.,
RA Letourneur F., Cosson P.;
RT "Synergistic control of cellular adhesion by transmembrane 9 proteins.";
RL Mol. Biol. Cell 14:2890-2899(2003).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=16367873; DOI=10.1111/j.1462-5822.2005.00607.x;
RA Benghezal M., Fauvarque M.O., Tournebize R., Froquet R., Marchetti A.,
RA Bergeret E., Lardy B., Klein G., Sansonetti P., Charette S.J., Cosson P.;
RT "Specific host genes required for the killing of Klebsiella bacteria by
RT phagocytes.";
RL Cell. Microbiol. 8:139-148(2006).
RN [5]
RP FUNCTION.
RX PubMed=25999474; DOI=10.1242/jcs.164848;
RA Perrin J., Le Coadic M., Vernay A., Dias M., Gopaldass N.,
RA Ouertatani-Sakouhi H., Cosson P.;
RT "TM9 family proteins control surface targeting of glycine-rich
RT transmembrane domains.";
RL J. Cell Sci. 128:2269-2277(2015).
CC -!- FUNCTION: Involved in adhesion, phagocytosis of hydrophilic particles
CC and intracellular killing of bacteria (PubMed:10944536,
CC PubMed:12857872, PubMed:16367873). Associates with proteins harboring
CC glycine-rich transmembrane domains and ensures their efficient
CC localization to the cell surface (PubMed:25999474).
CC {ECO:0000269|PubMed:10944536, ECO:0000269|PubMed:12857872,
CC ECO:0000269|PubMed:16367873, ECO:0000269|PubMed:25999474}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
CC {ECO:0000305}.
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DR EMBL; AJ318760; CAC47950.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73174.1; -; Genomic_DNA.
DR RefSeq; XP_647493.1; XM_642401.1.
DR AlphaFoldDB; Q55FP0; -.
DR STRING; 44689.DDB0191123; -.
DR TCDB; 8.A.68.1.4; the endomembrane protein-70 (emp70) family.
DR PaxDb; Q55FP0; -.
DR ABCD; Q55FP0; 4 sequenced antibodies.
DR EnsemblProtists; EAL73174; EAL73174; DDB_G0267444.
DR GeneID; 8616300; -.
DR KEGG; ddi:DDB_G0267444; -.
DR dictyBase; DDB_G0267444; phg1A.
DR eggNOG; KOG1278; Eukaryota.
DR HOGENOM; CLU_010714_4_1_1; -.
DR InParanoid; Q55FP0; -.
DR OMA; RWDLYFV; -.
DR PhylomeDB; Q55FP0; -.
DR PRO; PR:Q55FP0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:dictyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:dictyBase.
DR GO; GO:0010467; P:gene expression; IMP:dictyBase.
DR GO; GO:0007042; P:lysosomal lumen acidification; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:dictyBase.
DR GO; GO:0061462; P:protein localization to lysosome; IMP:dictyBase.
DR GO; GO:0072657; P:protein localization to membrane; IMP:dictyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:dictyBase.
DR GO; GO:0140460; P:response to Gram-negative bacterium; HDA:dictyBase.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR InterPro; IPR004240; EMP70.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10766; PTHR10766; 1.
DR Pfam; PF02990; EMP70; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..641
FT /note="Putative phagocytic receptor 1a"
FT /id="PRO_0000327715"
FT TOPO_DOM 24..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..608
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 604
FT /note="D -> Y (in Ref. 1; CAC47950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 73365 MW; FC342BC8D4183F71 CRC64;
MKINKKQIVF FILFSIFLNH VNGIFYLPGM IPHDFAQGEE GAIKVNKITS VHTQIPYKYY
QLPGVCQPKE GIIDDTENLG EILLGDRIEN SDYTFNFLTD GGKCKVINSE SCSPIIKKED
LKVLEDRIQN QYRVHWLLDG LPVRQTGRLA SDPGFDLGFM TLAEGQTVAT AEKYLNNHLE
ITIFYHSNPT DNTSRIVGFE IFPTSRQYKK VENWKGDTGD DCPQYGENFE QLSVSVKEGE
DQERFVLWTY EVKYTPSPVL WNKRWDIYFE SNDNSVHWFS ILNSLMIVFI LTVMVAMIII
RTLKKDIRRY TSIDTSEDRD SQEETGWKMI HGDVFRPPSH PMLLSVCIGS GVQIFSMTLI
TMIFAVLGFL SPANIGGLAT ALIVLFVLSA MFAGYFSTRV FTIFKGRNWK KNTIYTALSM
PGIIFGIFFF VNMFLRGAKS SAAVPFGTFA SIIAMWFGIS VPLVFLGSYF ASKKPVPEDP
VRTNQIPRQV PDQIWYMNPY LSILMGGILP FGAVFIELHF ILTSLWDNQF YYIFGFLFIV
LMILIVTSAE ISIVMCYFQL CAEDHHWWWR SFLTAGSSSL YMFIYSVSFF RYLGITKFIS
SLLDFSYSFI MSLAFAALTG TIGFYSCYFL VRKIYSSIHI N
