TGRD1_DICDI
ID TGRD1_DICDI Reviewed; 895 AA.
AC Q9U8Q1; C0JMQ2; C0JMQ3; C0JMQ4; C0JMQ5; C0JMQ6; C0JMQ7; C0JMQ8; C0JMQ9;
AC C0JMR1; C0JMR2; C0JMR3; C0JMR4; C0JMR5; C0JMR6; Q54L74;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Tiger protein D1;
DE AltName: Full=Loose aggregate C2 protein;
DE AltName: Full=Loose aggregate D1 protein;
DE AltName: Full=Transmembrane, IPT, Ig, E-set, Repeat protein D1;
DE Flags: Precursor;
GN Name=tgrD1; Synonyms=lagC2, lagD, lagD1; ORFNames=DDB_G0286825;
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], DISRUPTION PHENOTYPE, DEVELOPMENTAL
RP STAGE, AND VARIANTS ILE-27; VAL-247; LEU-359; ILE-424; ILE-455; ASN-591 AND
RP GLN-892.
RC STRAIN=QS11, QS113, QS15, QS18, QS21, QS23, QS32, QS34, QS36, QS38, QS4,
RC QS8, and QS9;
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 [MRNA].
RC STRAIN=AX3-1;
RA Takeda K., Saito T., Ochiai H.;
RT "Developmental regulated gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
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 DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=14651934; DOI=10.1016/j.ydbio.2003.08.025;
RA Kibler K., Svetz J., Nguyen T.-L., Shaw C., Shaulsky G.;
RT "A cell-adhesion pathway regulates intercellular communication during
RT Dictyostelium development.";
RL Dev. Biol. 264:506-521(2003).
CC -!- FUNCTION: May be involved in the regulation of aggregation. Activates
CC tgrC1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein; Extracellular side.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated; with a peak of
CC expression at 16 hours corresponding to the finger stage of
CC development. {ECO:0000269|PubMed:14651934,
CC ECO:0000269|PubMed:19285397}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to sporulate when in pure
CC population although they will sporulate when in chimerae with wild-type
CC cells. Cells form loose aggregate before disaggregating. Cells
CC aggregate and disperse repeatedly. After starvation, cells completely
CC fail to stream and display cAMP relay defects. Fail to rotate.
CC comC-/tgrC1-/tgrD1- triple mutants fail to form spores.
CC {ECO:0000269|PubMed:14651934, ECO:0000269|PubMed:19285397}.
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DR EMBL; FJ374953; ACN54212.1; -; Genomic_DNA.
DR EMBL; FJ374954; ACN54213.1; -; Genomic_DNA.
DR EMBL; FJ374955; ACN54214.1; -; Genomic_DNA.
DR EMBL; FJ374956; ACN54215.1; -; Genomic_DNA.
DR EMBL; FJ374957; ACN54216.1; -; Genomic_DNA.
DR EMBL; FJ374958; ACN54217.1; -; Genomic_DNA.
DR EMBL; FJ374959; ACN54218.1; -; Genomic_DNA.
DR EMBL; FJ374960; ACN54219.1; -; Genomic_DNA.
DR EMBL; FJ374961; ACN54220.1; -; Genomic_DNA.
DR EMBL; FJ374962; ACN54221.1; -; Genomic_DNA.
DR EMBL; FJ374963; ACN54222.1; -; Genomic_DNA.
DR EMBL; FJ374964; ACN54223.1; -; Genomic_DNA.
DR EMBL; FJ374965; ACN54224.1; -; Genomic_DNA.
DR EMBL; FJ374966; ACN54225.1; -; Genomic_DNA.
DR EMBL; FJ374967; ACN54226.1; -; Genomic_DNA.
DR EMBL; AB032076; BAA84094.1; -; mRNA.
DR EMBL; AAFI02000090; EAL64010.1; -; Genomic_DNA.
DR RefSeq; XP_637529.1; XM_632437.1.
DR AlphaFoldDB; Q9U8Q1; -.
DR STRING; 44689.DDB0191406; -.
DR PaxDb; Q9U8Q1; -.
DR EnsemblProtists; EAL64010; EAL64010; DDB_G0286825.
DR GeneID; 8625827; -.
DR KEGG; ddi:DDB_G0286825; -.
DR dictyBase; DDB_G0286825; tgrD1.
DR eggNOG; ENOG502RHZ3; Eukaryota.
DR HOGENOM; CLU_325837_0_0_1; -.
DR InParanoid; Q9U8Q1; -.
DR PhylomeDB; Q9U8Q1; -.
DR PRO; PR:Q9U8Q1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp 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; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..895
FT /note="Tiger protein D1"
FT /id="PRO_0000390621"
FT TOPO_DOM 22..861
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 883..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 295..381
FT /note="IPT/TIG 1"
FT DOMAIN 560..638
FT /note="IPT/TIG 2"
FT DOMAIN 642..725
FT /note="IPT/TIG 3"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
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 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 27
FT /note="T -> I (in strain: QS4, QS8, QS9, QS11, QS15, QS18,
FT QS21, QS23, QS32, QS34, QS36, QS38 and QS113)"
FT /evidence="ECO:0000269|PubMed:19285397"
FT VARIANT 247
FT /note="I -> V (in strain: QS4, QS8, QS9, QS11, QS15, QS18,
FT QS21, QS23, QS32, QS34, QS36, QS38 and QS113)"
FT /evidence="ECO:0000269|PubMed:19285397"
FT VARIANT 359
FT /note="P -> L (in strain: QS113)"
FT /evidence="ECO:0000269|PubMed:19285397"
FT VARIANT 424
FT /note="N -> I (in strain: QS23)"
FT /evidence="ECO:0000269|PubMed:19285397"
FT VARIANT 455
FT /note="V -> I (in strain: QS8, QS9, QS11, QS15, QS21 and
FT QS34)"
FT /evidence="ECO:0000269|PubMed:19285397"
FT VARIANT 591
FT /note="Y -> N (in strain: QS8, QS9, QS11, QS15, QS21 and
FT QS34)"
FT /evidence="ECO:0000269|PubMed:19285397"
FT VARIANT 892
FT /note="K -> Q (in strain: QS4, QS21, QS23, QS32, QS34 and
FT QS113)"
FT /evidence="ECO:0000269|PubMed:19285397"
SQ SEQUENCE 895 AA; 97644 MW; 5832A9A37B26B3FF CRC64;
MIHKMYFFLI LLFSLFIIVY SAPNRVTRNE TSIVYTYSLD SDYYTRFVMY LNATTLRTDI
APNYFDCSQI VNSERYCVFH FADSFSRLWG AVYSRVCTRT VSDPTEDCQS TWITDNAFPE
PLNVKFSGYP STSGGDVVFT GLFLRLAGGP NTLANSFTNP SKTFLIKVHG NFSDPNFNCN
NFTATFPPSS GYIKVYFDDT GKSSLQLRYA SPTVSSFILD ESKKLVTING DNYFTKNSLV
QVFFDGIIQN NINITVNHSQ IQVNNFIRVD PGPMSVNITI NAVSIDNNYT YCFPAVISSI
SSVSNHLGGV VTIKGSKLSS TSIIPTIKIG DKQCTFIKST TTELECQLEP NETGGKHLPV
DVNFGGCNST SSGSDAVTFT YSIPTLSSGT LSNGIVTLIG TNLGTINDSF IQLNSNGAID
NVKNDQFNIS SDETTATFKL PLLKCKSFYI NFTRVDISAN NKPSISAPLL IYVINKPTVS
NGSINIELYY IDCPISPSST PSITVGNSSS ATQCSIPSLK NLSEYYQTTC SIPYGTGTNK
QFKFKYNSEE SNSEFSYEPP KVESRSFSKG LFNITINGNN FGNSTSLIKV YFNGSDISSE
IQSLNDNQFT FKRLNSYENG PINITVDGNS NMEPSFYLTL PPVIYSIINK ENKTIGCGGL
ITISGKNLLT SDDKFKVRVL ANNENTTVIV PDEKTLIVRA NNKDSPLFVS TLIGDDLGPN
TTLTYFEPRI TVIPTVKNKK DGISIRVGGV SLSGIINASL GISSENVSLS CDLQCSLSPN
ETFYLSNPIL SSNEKDITNS TDCLSCHSMN SIVVDETSGV LYLQLGPTSY HYDVKIEEIQ
SSLNPSSSNG GERKSSKLSG GAIAGITIGC VAGAGALVGS VFYFKLITRV KKAFN
