TGRC1_DICDI
ID TGRC1_DICDI Reviewed; 889 AA.
AC P42523; Q54V08;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Tiger protein C1;
DE AltName: Full=Loose aggregate C protein;
DE AltName: Full=Loose aggregate C1 protein;
DE AltName: Full=Transmembrane, IPT, Ig, E-set, Repeat protein C1;
DE Flags: Precursor;
GN Name=tgrC1; Synonyms=gp150, lagC, lagC1; ORFNames=DDB_G0280531;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=7926779; DOI=10.1101/gad.8.8.948;
RA Dynes J.L., Clark A.M., Shaulsky G., Kuspa A., Loomis W.F., Firtel R.A.;
RT "LagC is required for cell-cell interactions that are essential for cell-
RT type differentiation in Dictyostelium.";
RL Genes Dev. 8:948-958(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3-1;
RA Shi H., Siu C.;
RT "Dictyostelium discoideum KAX-3 lagC gene.";
RL Submitted (APR-2000) 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=498273; DOI=10.1016/0092-8674(79)90058-8;
RA Geltosky J.E., Weseman J., Bakke A., Lerner R.A.;
RT "Identification of a cell surface glycoprotein involved in cell aggregation
RT in D. discoideum.";
RL Cell 18:391-398(1979).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=7407916; DOI=10.1016/0092-8674(80)90470-5;
RA Geltosky J.E., Birdwell C.R., Weseman J., Lerner R.A.;
RT "A glycoprotein involved in aggregation of D. discoideum is distributed on
RT the cell surface in a nonrandom fashion favoring cell junctions.";
RL Cell 21:339-345(1980).
RN [6]
RP FUNCTION.
RX PubMed=3063296; DOI=10.1139/o88-126;
RA Siu C.-H., Wong L.M., Lam T.Y., Kamboj R.K., Choi A., Cho A.;
RT "Molecular mechanisms of cell-cell interaction in Dictyostelium
RT discoideum.";
RL Biochem. Cell Biol. 66:1089-1099(1988).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1577768; DOI=10.1016/s0021-9258(19)50438-0;
RA Gao E.N., Shier P., Siu C.-H.;
RT "Purification and partial characterization of a cell adhesion molecule
RT (gp150) involved in postaggregation stage cell-cell binding in
RT Dictyostelium discoideum.";
RL J. Biol. Chem. 267:9409-9415(1992).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11071787; DOI=10.1006/dbio.2000.9881;
RA Wang J., Hou L., Awrey D., Loomis W.F., Firtel R.A., Siu C.-H.;
RT "The membrane glycoprotein gp150 is encoded by the lagC gene and mediates
RT cell-cell adhesion by heterophilic binding during Dictyostelium
RT development.";
RL Dev. Biol. 227:734-745(2000).
RN [9]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11792801; DOI=10.1242/jcs.114.24.4349;
RA Coates J.C., Harwood A.J.;
RT "Cell-cell adhesion and signal transduction during Dictyostelium
RT development.";
RL J. Cell Sci. 114:4349-4358(2001).
RN [10]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
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).
RN [11]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=15561583; DOI=10.1016/j.semcdb.2004.09.004;
RA Siu C.-H., Harris T.J.C., Wang J., Wong E.;
RT "Regulation of cell-cell adhesion during Dictyostelium development.";
RL Semin. Cell Dev. Biol. 15:633-641(2004).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: tgrB1 and tgrC1 are involved in kin discrimination. They play
CC an essential role in aggregation and subsequent development. Could
CC function as a non-diffusible cell-cell signaling molecule that is
CC required for multicellular development. Has both cell-autonomous and
CC non-cell-autonomous functions. Terminal node, epistatic both to comC
CC and tgrD1. Activates tgrD1. {ECO:0000269|PubMed:11071787,
CC ECO:0000269|PubMed:11792801, ECO:0000269|PubMed:14651934,
CC ECO:0000269|PubMed:1577768, ECO:0000269|PubMed:19285397,
CC ECO:0000269|PubMed:3063296, ECO:0000269|PubMed:498273}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11071787,
CC ECO:0000269|PubMed:15561583, ECO:0000269|PubMed:1577768,
CC ECO:0000269|PubMed:498273, ECO:0000269|PubMed:7407916}; Single-pass
CC type I membrane protein {ECO:0000255}. Cell junction
CC {ECO:0000269|PubMed:11071787, ECO:0000269|PubMed:15561583,
CC ECO:0000269|PubMed:1577768, ECO:0000269|PubMed:7407916}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in the mid-aggregation
CC stage, followed by a rapid increase that coincides with the completion
CC of aggregate formation. Expression is greatest in cells at the
CC periphery and the rear end of the migrating slug.
CC {ECO:0000269|PubMed:11792801, ECO:0000269|PubMed:14651934,
CC ECO:0000269|PubMed:15561583}.
CC -!- INDUCTION: Induced at the loose aggregate stage and expressed through
CC the remainder of development.
CC -!- DISRUPTION PHENOTYPE: Mutant cells are unable to sporulate in isolation
CC although they will sporulate when in the presence of wild-type cells.
CC Cells form loose aggregates before disaggregating. After starvation,
CC cells form wide streams that frequently break and form secondary
CC centers before reaching the primary center and display cAMP relay
CC defects. Cells fail to rotate. tgrB1 and tgrC1 double mutants show
CC strain segregation in chimeras with wild-type cells. ComC, tgrC1 and
CC tgrD1 triple mutants fail to form spores. {ECO:0000269|PubMed:11071787,
CC ECO:0000269|PubMed:14651934, ECO:0000269|PubMed:19285397}.
CC -!- MISCELLANEOUS: The tgrC1 gene is highly polymorphic.
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DR EMBL; U09478; AAA18494.1; -; mRNA.
DR EMBL; AF258615; AAF72532.1; -; Genomic_DNA.
DR EMBL; AAFI02000037; EAL67067.1; -; Genomic_DNA.
DR PIR; A54280; A54280.
DR RefSeq; XP_641123.1; XM_636031.1.
DR AlphaFoldDB; P42523; -.
DR STRING; 44689.DDB0214927; -.
DR PaxDb; P42523; -.
DR EnsemblProtists; EAL67067; EAL67067; DDB_G0280531.
DR GeneID; 8622682; -.
DR KEGG; ddi:DDB_G0280531; -.
DR dictyBase; DDB_G0280531; tgrC1.
DR eggNOG; ENOG502RHZ3; Eukaryota.
DR HOGENOM; CLU_325837_0_0_1; -.
DR InParanoid; P42523; -.
DR OMA; KEPRTEM; -.
DR PhylomeDB; P42523; -.
DR PRO; PR:P42523; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IDA:dictyBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:dictyBase.
DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0099138; P:altruistic, chimeric sorocarp development; IDA:dictyBase.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IGI:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IDA: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:0090073; P:positive regulation of protein homodimerization activity; IDA:dictyBase.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:dictyBase.
DR GO; GO:1902168; P:response to catechin; IDA:dictyBase.
DR GO; GO:0099120; P:socially cooperative development; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IGI:dictyBase.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..889
FT /note="Tiger protein C1"
FT /id="PRO_0000021575"
FT TOPO_DOM 20..851
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..889
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 120..207
FT /note="IPT/TIG 1"
FT DOMAIN 293..380
FT /note="IPT/TIG 2"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
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 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 322..323
FT /note="SS -> YY (in Ref. 1; AAA18494 and 2; AAF72532)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..337
FT /note="VCKF -> YVI (in Ref. 1; AAA18494 and 2; AAF72532)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="S -> R (in Ref. 1; AAA18494 and 2; AAF72532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 889 AA; 97443 MW; 92C5CF0DDF82CD1E CRC64;
MEKKIILLIL FLFFISGYSM NPPTPIDAIY DDKSFTLIFN SNLPYSTRLI LYKNEKEPRT
EMAPNYFNCS LVDGERHCLF HSDEPFSRLW GSIDSKVCVR DKSNTVEDCT FDASGLVYYP
KVYNLKYSKK PKTSGEDIVI TGSYLRLFGG PNFLINSIDV NKPFVVKGNF SDPSFDCNNI
TVTFPPGSGK FRLYYDETGD NPVPFSYESP IISSSVSDSS KQIITINGDN FFTDKDLVKV
SFDGIDQPNF IISVNHKQIQ VNNYNRVDPG PMSVNITVDE VSIEKNYIHC FPAIITSISS
VSNHLDGIVT IKGEKLSSTL NSSLTPSITI GDKVCKFIKS TTTELECKLD ANELGGKNLP
VNVNFGGCDS TSPNGVSFTY NIPTLSSGSY SNGIVTLIGT NLGTNNESSI QLYGDGIKNT
NISQFNVSSS DEKSVTFELP HLRCRSFNIN FTRSGITAKT LSISASLSVN VINRPTVSNG
ILNIEIYYMD CTISSSAPSI TVGDSSSASP CSIPSSNSSY YETTCPTPYG TGINKQFIFK
LNSETVSDQF SYAPPEVENR TISDDGTNIE LHGNNFGNST SLIKVYLNGS DISSEIQELE
DHQLTIKILD SYENGPINIT VDGNYMDSLF YLTLPPVIYR ITNKDNKTLA CGGLITVSGK
NLLTSDKEFK VNVKSNNKNT TVFAQDEKIL IVRDESRESS LFVTTFIGVR SGPSTTLTYI
KPMISEIPTI ENKIEKGILA IIRGYSFTDI LNASLTVSSE TVPLSCNLEC SLSPNEILDD
SDSSETNITN SNTDCLSCHS GSSVKNTSGV LYLLFNSTSF QYNVTIEEIK LSPSPNVSQR
DVETKSSKPS NGLIIGSTIG SVGGALAIGA LAYYFKIPFR VKKFIGKKF
