G13A_DICDI
ID G13A_DICDI Reviewed; 730 AA.
AC P34115; Q54GA6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Cell surface glycoprotein gp138A;
DE Flags: Precursor;
GN Name=GP138A; Synonyms=fusA; ORFNames=DDB_G0290257;
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 PROTEIN SEQUENCE OF 21-32.
RC STRAIN=AX3;
RX PubMed=7680629; DOI=10.1006/dbio.1993.1070;
RA Fang H., Higa M., Suzuki K., Aiba K., Urushihara H., Yanagisawa K.;
RT "Molecular cloning and characterization of two genes encoding gp138, a cell
RT surface glycoprotein involved in the sexual cell fusion of Dictyostelium
RT discoideum.";
RL Dev. Biol. 156:201-208(1993).
RN [2]
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).
CC -!- FUNCTION: Involved in the sexual cell fusion of D.discoideum.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- DEVELOPMENTAL STAGE: Expressed at the time of acquisition of fusion
CC competence of cells.
CC -!- PTM: The sugar chains may play important roles in cell fusion.
CC -!- PTM: The GPI-like-anchor contains a phosphoceramide group, rather than
CC a phosphatidyl group. {ECO:0000305}.
CC -!- MISCELLANEOUS: gp138a expression is much higher than that of gp138b and
CC may well be the major gene for gp138 product.
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; D12883; BAA02287.1; -; Genomic_DNA.
DR EMBL; AAFI02000162; EAL62255.1; -; Genomic_DNA.
DR PIR; A48832; A48832.
DR RefSeq; XP_635777.1; XM_630685.1.
DR AlphaFoldDB; P34115; -.
DR SMR; P34115; -.
DR PaxDb; P34115; -.
DR EnsemblProtists; EAL62255; EAL62255; DDB_G0290257.
DR GeneID; 8627582; -.
DR KEGG; ddi:DDB_G0290257; -.
DR dictyBase; DDB_G0290257; cfrA.
DR HOGENOM; CLU_022518_0_0_1; -.
DR InParanoid; P34115; -.
DR OMA; VECEYIN; -.
DR PhylomeDB; P34115; -.
DR PRO; PR:P34115; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006907; P:pinocytosis; IBA:GO_Central.
DR GO; GO:0140084; P:sexual macrocyst formation; IGI:dictyBase.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF01833; TIG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7680629"
FT CHAIN 21..708
FT /note="Cell surface glycoprotein gp138A"
FT /id="PRO_0000021306"
FT PROPEP 709..730
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021307"
FT DOMAIN 504..592
FT /note="IPT/TIG"
FT REPEAT 683..686
FT /note="1"
FT REPEAT 687..690
FT /note="2"
FT REPEAT 691..694
FT /note="3"
FT REGION 678..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..694
FT /note="3 X 4 AA tandem repeats of P-S-T-T"
FT COMPBIAS 679..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 708
FT /note="GPI-like-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 730 AA; 80961 MW; C2BDB82BC24CD133 CRC64;
MKIILILSIF LICFLQLGQS VIDPSQNEVM SDLLFNLYGY DKSLDPCNNN YVECEYINTT
STIQTVKSLS LGAPLHQYVI TQDLTPLQNL TSFEVNEKIY LTSSFFNYIN KFSQLERIVT
YSLNLTIPDD TIFPAIFETF TIYKPSVPLS KVIFESPIKN LYVDSPLTGY SIPTLVNVNP
YLGNLQLPVT YYSGFPSNLS QAFPNLQYLA IYVNNDMNQN NYHNFSISNI GVFKNLKGLD
IEFTDSDNPQ EFSIHSFLSN VPIIDNLYIY GQGVTIDPSV GIIDLSYINP KTFLKIQIQQ
TSLLNNCKGI ILKSPKKASF NSYYNTFSYE CIDFSNIADF SDYYNDYEQY LPNIDNAPLL
TGVDIYQSVV VGDIPESYCR INYLSLYYNQ LNGTVPSCIQ CLGGVKGGDI VLPNPFLNFN
KTTEPYCPTF KIDENYTHLV ATDGTEKLII TGTNLGWDGN DITPIIANSK LGITIPKGVG
TNKSITVTFQ NGEQRTFNYS YVPPFIKSYG FLELDGHKYF TINGTGFDFV DSNNITINDQ
QITFDNAMGG GDNDGLIIFP IDELPNFATE SKFTVSALVG GQSSNEVTFY YFNSINITEE
KLVLNNTGGS VDINGSFGTN NTSLVSVSIN GTNCLVTSYT NSKLTITYPS NQVGDNYVLT
LNVGGYAVNL VVEYIEGGET PTPSTTPSTT PSTTPSSTPT QSPDDDGSTS STLSTSFYLI
TLLFLIQQFI
