TAGC_DICDI
ID TAGC_DICDI Reviewed; 1741 AA.
AC Q23868; Q54M84;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine protease/ABC transporter B family protein tagC;
DE EC=3.4.21.-;
DE AltName: Full=Prestalk-specific protein tagC;
DE Flags: Precursor;
GN Name=tagC; ORFNames=DDB_G0286121;
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], FUNCTION, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX4;
RX PubMed=8986798; DOI=10.1073/pnas.93.26.15260;
RA Shaulsky G., Escalante R., Loomis W.F.;
RT "Developmental signal transduction pathways uncovered by genetic
RT suppressors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15260-15265(1996).
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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9473320; DOI=10.1006/dbio.1997.8804;
RA Anjard C., Zeng C., Loomis W.F., Nellen W.;
RT "Signal transduction pathways leading to spore differentiation in
RT Dictyostelium discoideum.";
RL Dev. Biol. 193:146-155(1998).
RN [4]
RP FUNCTION.
RX PubMed=16672332; DOI=10.1242/dev.02399;
RA Anjard C., Loomis W.F.;
RT "GABA induces terminal differentiation of Dictyostelium through a GABAB
RT receptor.";
RL Development 133:2253-2261(2006).
CC -!- FUNCTION: May be directly involved in maturation and export of SDF-2.
CC The exposure of the protease domain of tagC on the surface of the
CC prestalk cells were it can convert acbA to SDF-2 is induced by GABA.
CC Intercellular communication via tagC may mediate integration of
CC cellular differentiation with morphogenesis.
CC {ECO:0000269|PubMed:16672332, ECO:0000269|PubMed:8986798,
CC ECO:0000269|PubMed:9473320}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DEVELOPMENTAL STAGE: Found exclusively in prestalk cells.
CC {ECO:0000269|PubMed:8986798}.
CC -!- DISRUPTION PHENOTYPE: Cells in which tagC is disrupted do not form SDF-
CC 2. Null mutations in either tagB or tagC lead to a cell autonomous
CC defect in prestalk differentiation and a 5-fold reduction in the
CC expression of the prestalk gene ecmA. Disruption of regA in a tagB null
CC or in a tagC null background results in higher levels of sporulation.
CC {ECO:0000269|PubMed:8986798, ECO:0000269|PubMed:9473320}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ABC transporter
CC superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201)
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peptidase S8
CC family. {ECO:0000305}.
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DR EMBL; U60086; AAB03331.1; -; mRNA.
DR EMBL; AAFI02000085; EAL64353.1; -; Genomic_DNA.
DR PIR; T18279; T18279.
DR RefSeq; XP_637864.1; XM_632772.1.
DR AlphaFoldDB; Q23868; -.
DR SMR; Q23868; -.
DR STRING; 44689.DDB0191192; -.
DR MEROPS; S08.127; -.
DR PaxDb; Q23868; -.
DR PRIDE; Q23868; -.
DR EnsemblProtists; EAL64353; EAL64353; DDB_G0286121.
DR GeneID; 8625461; -.
DR KEGG; ddi:DDB_G0286121; -.
DR dictyBase; DDB_G0286121; tagC.
DR eggNOG; KOG0055; Eukaryota.
DR eggNOG; KOG0058; Eukaryota.
DR HOGENOM; CLU_235711_0_0_1; -.
DR InParanoid; Q23868; -.
DR OMA; STCLELM; -.
DR PhylomeDB; Q23868; -.
DR Reactome; R-DDI-1369007; Mitochondrial ABC transporters.
DR Reactome; R-DDI-159418; Recycling of bile acids and salts.
DR Reactome; R-DDI-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-9754706; Atorvastatin ADME.
DR PRO; PR:Q23868; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IMP:dictyBase.
DR GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
DR GO; GO:0016485; P:protein processing; IMP:dictyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.200; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Hydrolase; Membrane; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1741
FT /note="Serine protease/ABC transporter B family protein
FT tagC"
FT /id="PRO_0000027192"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1072..1092
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1157..1177
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1260..1280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1288..1308
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 297..729
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 1031..1314
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1450..1687
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1334..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 637
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 1485..1492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
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 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 597
FT /note="D -> A (in Ref. 1; AAB03331)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="V -> D (in Ref. 1; AAB03331)"
FT /evidence="ECO:0000305"
FT CONFLICT 1740..1741
FT /note="QV -> KFKN (in Ref. 1; AAB03331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1741 AA; 193884 MW; 44DEC61D68E4947D CRC64;
MKFHFSSNKL LLISGLILLV LVIGIKLDIF LSSKSTEYIK FNNNNNHFKR DKRILLHNEI
IDTNNKPSIK NNQIFINDND NNENISPILL RILNNNNNNN NNNGDDKSIY KKNHYIVQFK
DRINDETREQ LKEFLIGTDI VLDEQPYQSH IVHYIPHDSF LVLMTQEQSV LLSSKEWVSW
IGEFEPSNKI HLNYNEKSIG LPVYIILSDS TNSLIQRWEN TLNSILKSYN SKVKLTLINQ
KKLKSIVYCN DESPSPSCSL INSEKLVYQW ISEQSESNFI ERSEKFQTAN RLSPKVVFGT
KDTLVNNDRV DIPLRGKGQI LSIADTGLDG SHCFFSDSKY PIPLNSVNLN HRKVVTYITT
STSDDSDKVD GHGTHICGSA AGTPEDSSVN ISSFSGLATD AKIAFFDLAS GSSSLTPPSD
LKQLYQPLYD AGARVHCDSW GSVSVEGYTG SYSSDTASID DFLFTHPDFI ILRAAGNNEQ
YLSLLTQSTA KNVITVGAHQ TIHENYLTDG PNYINYQSSV DINQELICDF DSRYCNYTTA
QCCLESNATT GLASCCPTLL RKSVIDAANT QPLLYNENNI CSFSSKGPTH DGRMKPDLVA
PGEYITSARS NGANTTDQCG DGSLPNTNAL LAISGTSMAT SFAAAATTIL RQYLVDGYYP
TGSIVESNKL QPTGSLLKAL MINNAQLLNG TFQLITSSSI TYPSNQVFEN FAGASLVQGW
GAIRMSNWLH VVNNNNSNNN NKTSDGITKF VGIGGLDLRL VKPNQWKEES LSTGQNTSYC
FTYKPSSSSS NSGNNIPRVV ATLVWTDPPS YAGAKFNLVN NLDLTMIYYR DNGSTIFYSN
QGGSSFLGLA PTQDTLNNVE GIVHNPTEPM TYRFMVAGTN VPMGPQNFSF VFHGENGEFE
WADKCPQCSP GQVLACPVEN GIGTQLCTSD LQWSSCLIQS CDNNYNYNSI KKRCDKFLSY
NYIIMIVAGG TMLLIIFILL LIKYQEYKES KKDSFRRFDD GTGIFVRPKD KDAKVSLADL
YNLISPFIIE LAISTACSLV STAASILQPF YIGQIINDIP TAKHIGDFKS QFILIFILAV
IEFVFSTISS WISGIVNEKM VMRLQNKVFR ALIAQDMGFF QKNNAAILMN VLISDTPMLR
SALTGILLSI ATGLCKFVGS LVFIFTISWK LSLVFFATVP VLAFITQIQS QFTKRLTRAL
LFYNSKASQH GQESMVNMHV VTNYCRQDKE IIKYTDNLNN VFQTARRLII NNTLASSIKW
LMVESLAFII LYYGAYLAIQ KQFTVGLLIS FCLYIGYVID STTTLFGVYV SYVQSQASAT
RVFMILRSAP RKRTTLEEEE ADRNNGLGGG GGNNNNNDDD DDDDNYNGKG NDNGKGSDDP
NNNNNNTTLE NIDDNGELTT VQPVELTKKQ LKKQKEKEQK EYFKRTGISV VEMSLIPSSY
IELTDCKGEI EFKNVSFRYP TRPDVQVLHN INMKFETGKC YGLVGPSGSG KSTLLELISK
FYPLRDGGNI IMDDIDIANI RPNNLRGFVT CVHQNPYLFD ASIKDNIGYA LDNPTIEEVI
EAAKLAYAHE FIKDLPQQYD TVLGSAGSLL SGGQKKRIAI ARAICAKRKI MLLDEITAEL
DPESEEAITQ SIKVLTQGHT VVMVAHKVAA VRDCDKIFVL DKGYLVEEGT HDELMERKGK
YHRMFNNEKD EEELLNNLGL PSNNETNNEN NNENNNNNNN NNNNNNNNND DNNNQVVGEQ
V
