G13B_DICDI
ID G13B_DICDI Reviewed; 734 AA.
AC P34116; Q54GA3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Cell surface glycoprotein gp138B;
DE Flags: Precursor;
GN Name=GP138B; Synonyms=fusB; ORFNames=DDB_G0290259;
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 -!- 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; D12884; BAA02288.1; -; Genomic_DNA.
DR EMBL; AAFI02000162; EAL62256.1; -; Genomic_DNA.
DR RefSeq; XP_635780.1; XM_630688.1.
DR AlphaFoldDB; P34116; -.
DR SMR; P34116; -.
DR PaxDb; P34116; -.
DR EnsemblProtists; EAL62256; EAL62256; DDB_G0290259.
DR GeneID; 8627585; -.
DR KEGG; ddi:DDB_G0290259; -.
DR dictyBase; DDB_G0290259; cfrB.
DR HOGENOM; CLU_022518_0_0_1; -.
DR InParanoid; P34116; -.
DR OMA; VECDDIN; -.
DR PhylomeDB; P34116; -.
DR PRO; PR:P34116; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central.
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; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
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 gp138B"
FT /id="PRO_0000021308"
FT PROPEP 709..734
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021309"
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 REPEAT 695..698
FT /note="4"
FT REGION 678..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..698
FT /note="4 X 4 AA tandem repeats of P-S-T-T"
FT COMPBIAS 679..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 708
FT /note="GPI-like-anchor amidated glycine"
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 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 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 734 AA; 81063 MW; 89F7877C84EEE11A CRC64;
MKIILTLSIF LICFLQLGQS VIDPSQNEVM SDLLFNLYGY DKSLDPCNSN SVECDDINST
STIKTVISLN LPTPLQEYVI TQDLTPLQNL TYMELYEKIY LTLSFFKNIN KLTQLETIVT
LSFNVTIPDD TIFPASLETF SIYKPSVPLS IAIFGSNIKN LYVNSPLTGY SIPTLINVNP
YLENLQLPVT YYSGFPSNIS LAFPNLQYLT IYVNNDMDQN NYHNFSISNI GVFKNLKGLD
IEFTDSYNPQ EFSINSFLSN VPVIDSLYIY GQGVTIDPSV GIIDLSYVKS KKFLSINIQE
SSLLNNCKGK SFKSPKKAYF RSNYNTFSYA CIDFSNLAYF YDYYNEYEQY LPNIDNAPLL
NEIYISESVV VGDIPESYCR INYLGLNYNQ LNGTAPSCIL CLGGNRGGDI VLPNPLLNFN
KTSEPYCPTF KIDQNYTNLV ATDGIGKLII TGTNLGWYGN DITPITANSK LAITIPKGVG
TNKSITVTFQ NGEQRTFNYS YVPPFIKSYG FLELDSNKYL TINGTGFDFE NPNIITINGQ
QITFSIALGG GDNDGLIALP IDELPNFDSE TKFTVSTLVG GQSSNEVTFY YFNSINITEE
KLVLNNTGGS VDINGSFGTN NISLVSISIN GTNCLVTSYT NSKLTIQYPS KQVGDNYVLT
LNVGGYAVNL VVEYIEGGET PTPSTTPSTT PSTTPSTTPS STPTQSPGDD GSTSSTLSIS
FYLITLLLLT QQFI
