TGRB1_DICDI
ID TGRB1_DICDI Reviewed; 902 AA.
AC Q54V07;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Tiger protein B1;
DE AltName: Full=Loose aggregate B1 protein;
DE AltName: Full=Transmembrane, IPT, Ig, E-set, Repeat protein B1;
DE Flags: Precursor;
GN Name=tgrB1; Synonyms=lagB, lagB1; ORFNames=DDB_G0280689;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX4;
RX PubMed=19285397; DOI=10.1016/j.cub.2009.02.037;
RA Benabentos R., Hirose S., Sucgang R., Curk T., Katoh M., Ostrowski E.A.,
RA Strassmann J.E., Queller D.C., Zupan B., Shaulsky G., Kuspa A.;
RT "Polymorphic members of the lag gene family mediate kin discrimination in
RT Dictyostelium.";
RL Curr. Biol. 19:567-572(2009).
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: tgrB1 and tgrC1 are involved in kin discrimination. They play
CC an essential role in aggregation and subsequent development.
CC {ECO:0000269|PubMed:19285397}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: TgrB1 and tgrC1 double mutants show strain
CC segregation in chimeras with wild-type cells.
CC {ECO:0000269|PubMed:19285397}.
CC -!- MISCELLANEOUS: The tgrB1 gene is highly polymorphic.
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DR EMBL; FJ374904; ACN71254.1; -; Genomic_DNA.
DR EMBL; AAFI02000037; EAL67146.1; -; Genomic_DNA.
DR RefSeq; XP_641124.1; XM_636032.1.
DR AlphaFoldDB; Q54V07; -.
DR STRING; 44689.DDB0266979; -.
DR PaxDb; Q54V07; -.
DR EnsemblProtists; EAL67146; EAL67146; DDB_G0280689.
DR GeneID; 8622683; -.
DR KEGG; ddi:DDB_G0280689; -.
DR dictyBase; DDB_G0280689; tgrB1.
DR eggNOG; ENOG502RI4S; Eukaryota.
DR HOGENOM; CLU_325834_0_0_1; -.
DR OMA; MWDIALE; -.
DR PhylomeDB; Q54V07; -.
DR PRO; PR:Q54V07; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IDA:dictyBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IEP:dictyBase.
DR GO; GO:0099138; P:altruistic, chimeric sorocarp development; IDA:dictyBase.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IGI:dictyBase.
DR GO; GO:0009988; P:cell-cell recognition; IMP:dictyBase.
DR GO; GO:0097656; P:cell-cell self recognition; IGI:dictyBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:dictyBase.
DR GO; GO:0099120; P:socially cooperative development; IMP:dictyBase.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR Pfam; PF01833; TIG; 2.
DR SUPFAM; SSF81296; SSF81296; 2.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..902
FT /note="Tiger protein B1"
FT /id="PRO_0000393399"
FT TOPO_DOM 25..803
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 249..323
FT /note="IPT/TIG 1"
FT DOMAIN 603..680
FT /note="IPT/TIG 2"
FT DOMAIN 704..788
FT /note="IPT/TIG 3"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 902 AA; 100319 MW; C9D20810A1CBD617 CRC64;
MKVIYIYLLL LLVCKFLFVK SSCSLKVGKI ECTKELETFL LYNETVVNVK MDTNGVKYYF
NALEFPYKNL LCDLNIDIKF TPEIPSFPNI PTTGGDFGFT FNFPCDYRRR VKRIEIERTI
LSLSFDTSKN QFVTYLNPGC GPFNISSSGI QILSTTYETG AIPNVPILDD DKGILTIQGS
NLYNTSIKIY SNNILKDTNP SGALDASHSS VTFSAEEFLT PNNWTIEVSI CGSFYKSYSF
PYFPKLDKME GVLNDNGGNM VFTGKHLRPK HNVTGTFGNK TIECLTSNSS KSITCTIPSR
KNYGFLGYDI PVTITIDGEY KSNTIKISYD LPLIQSVSQR GNSQIFDVTG VYFSGVKNMT
VITGKNMKTD IIQKKTATLE EPGFFIESNY TIFIFLPNNT QPGFMNLVVG DGGSETFTSP
RYNFKITPTI TAGQTFNSTT SGNDLEIKGI FMRTVDSDGR DVPLTVNSGS GGLVCNPLKD
GDGLLFTCVL GPGFGSSHTM NVYYNLIPIG SFTVSYNPPY LGTSEQEKDG TIKMNGKDLG
ESVKDSIMTV VYSDGNTVNG TVIKSSHTSL IFRYPIGNRN TASYIFQLGD QKSNKAGPFT
LKPIIENTDP AVPCGGGVVT INGHYFFNYT KDTTTITIGK VPCNISSISE TTIECVIVPN
LRSLSPYYTS GTKPLVISSS NPGTEKVYQL TPAGLNYKFA PPTITNTSAI DQTALITIYG
TSFGDANLEI LINDKPCTQP EINIHTYSSL TCNVTNYDEM KIYNYSNTKF NISISVDGQY
FIADIFQFKY ESGIIYSENK STGFPNEMYL GFVVFVIFIA LISFAAKNQI EKYFEERKSR
KAFRSLDNLR LKLRQKHATE IAKHYTFGEQ SAPKPDKSTF YDIRKKLSRL PLIRRCFKEH
TD
