TAGA_DICDI
ID TAGA_DICDI Reviewed; 1752 AA.
AC Q9GTN7; Q54C91;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine protease/ABC transporter B family protein tagA;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=tagA; ORFNames=DDB_G0293002;
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, SYNTHESIS OF 1623-1642, DISRUPTION
RP PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=12756178; DOI=10.1242/dev.00523;
RA Good J.R., Cabral M., Sharma S., Yang J., Van Driessche N., Shaw C.A.,
RA Shaulsky G., Kuspa A.;
RT "TagA, a putative serine protease/ABC transporter of Dictyostelium that is
RT required for cell fate determination at the onset of development.";
RL Development 130:2953-2965(2003).
RN [2]
RP SEQUENCE REVISION TO 994 AND 1681-1752.
RA Good J.R., Cabral M., Kuspa A.;
RL Submitted (OCT-2004) 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.
RX PubMed=17056744; DOI=10.1128/ec.00287-05;
RA Cabral M., Anjard C., Loomis W.F., Kuspa A.;
RT "Genetic evidence that the acyl coenzyme A binding protein AcbA and the
RT serine protease/ABC transporter TagA function together in Dictyostelium
RT discoideum cell differentiation.";
RL Eukaryot. Cell 5:2024-2032(2006).
RN [5]
RP INDUCTION.
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
CC -!- FUNCTION: Required for a general cell fate determination at the onset
CC of development. Required for the specification of an initial population
CC of prespore cells in which tagA is expressed. Required for normal SDF-2
CC signaling during spore encapsulation. {ECO:0000269|PubMed:12756178,
CC ECO:0000269|PubMed:17056744}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DEVELOPMENTAL STAGE: Expressed in prespore and in mature spores, and at
CC low levels in vegetative cells. Accumulates between 2 and 10 hours of
CC development and decreases thereafter (at protein level).
CC {ECO:0000269|PubMed:12756178}.
CC -!- INDUCTION: Down-regulated by phagocytic stimuli (when grown on E.coli).
CC {ECO:0000269|PubMed:18559084}.
CC -!- DISRUPTION PHENOTYPE: TagA mutant aggregates elaborate multiple
CC prestalk cell regions during development and produce spores
CC asynchronously and with low viability. They produce about twice as many
CC prestalk cells as the wild type as judged by a prestalk cell reporter
CC construct. When mixed with wild-type cells, tagA-cells become
CC overrepresented in the prestalk cell population, suggesting that this
CC phenotype is cell-autonomous. {ECO:0000269|PubMed:12756178}.
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; AF263455; AAG11416.2; -; mRNA.
DR EMBL; AAFI02000199; EAL60853.1; -; Genomic_DNA.
DR RefSeq; XP_629328.1; XM_629326.1.
DR AlphaFoldDB; Q9GTN7; -.
DR SMR; Q9GTN7; -.
DR STRING; 44689.DDB0229852; -.
DR MEROPS; S08.128; -.
DR TCDB; 3.A.1.201.40; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q9GTN7; -.
DR PRIDE; Q9GTN7; -.
DR EnsemblProtists; EAL60853; EAL60853; DDB_G0293002.
DR GeneID; 8629052; -.
DR KEGG; ddi:DDB_G0293002; -.
DR dictyBase; DDB_G0293002; tagA.
DR eggNOG; KOG0058; Eukaryota.
DR HOGENOM; CLU_239373_0_0_1; -.
DR InParanoid; Q9GTN7; -.
DR OMA; TIWNGIY; -.
DR PhylomeDB; Q9GTN7; -.
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:Q9GTN7; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
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; IGC:dictyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IGC:dictyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; 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; -; 1.
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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Differentiation; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1752
FT /note="Serine protease/ABC transporter B family protein
FT tagA"
FT /id="PRO_0000391321"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1058..1078
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1102..1122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1174..1194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1200..1220
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1315..1335
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 280..696
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 1059..1341
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1374..1610
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 946..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 625
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 1409..1416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
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 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1752 AA; 192812 MW; 3B1BD61844322380 CRC64;
MNKKLFIFGL SLFLFLFIFN LSLSLKLSSK NNFYNHNHIN NQIHRNNEGN NKLSKLIHLH
NDVIDTTISN RDNILFNKKS LNQKSKGSLF LVHLNGPIEK QVHNELIKQL DQLFNGGEII
HYIPDNTYLI SMIGSDNNDN NNNNKIELIN RLKELIPSIQ WLKPLEPRLK ISPLFKQNQF
QGDNQNEIDQ LRIYYHENSN QQSNDIDNII SESSLTLVEK ELISNNNNNN NNVLITVNLK
NSKLSLESII YKISTRSLVY WIEPSSSKLI KHTPSNKFAH YSIQSGSAST TSTPIWDVIG
IKGDGEIVGC ADTGIDINHC FFYDTNPIGS THRKIISYSS GNGDQIDEID GHGTHIVGTI
IGSTTVDPSV SEFSGGAPNS KVAFVDLQVG SGNGLSIQSN LTAIYQSTYD QNAKVHCDAW
NSNIGPFYTG VTEMIDRFQW DHPDFLVVRS AGNNVNFGFN SIYTLSQEST SKNSLVVGSS
NQPSSTYLSS IDYWDWDFIY NSIRTSVCTQ GQSIYGITCS DVPTQTTSVD IQTQCCSNPI
LAKICCSTEI QQQYQTNSTV YSEFIPSLFS GVGPTSDGRL KPDLLAPGSP IISSRSLGPS
STINHCSPIT SGIATSALIA MEGSSQAAAV ATSAAVLVRQ YYRDGYFING KVNSSVGFQP
SASLVKATLI NTASINVDST LEYSQGFGNI QLSKLITTTN AQTTSLDIPS SIEKADPIIN
TGETNSYCFS LDSKADIDIT LVWTDPAGSP LSTFTLVNNL DLALLAFVDG ELSIYSGNSE
TIFKNTSQVI FDQLNNVEVI RIKDAPIGSY DVKIFGTNIV IPNQSYSVVI RTSGGTTLMK
ESECAQCFYD PNDDQSQMCE FDNGIGTQYC KDDNRFSKCV VYECNTGYVF DNGITKSCVT
TLALTLYDIV LLGIFGIIIV GAVIFVLVCY KSKSLDQNKY FSLSKDKGGD GNSIRSNSVA
GNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNSNGKQS NIELNSVGGG DDGTPNGDDQ
QQQNNSPQYD EDGRLISGQE VEISIFEVIS LGKPESKILG LALFLSFIDV ALGLAVPLVA
ANIFDYLYAG ETGKISTTIL TFALIIIGMI IVQFLSGILL ALAGHRIIAR LRREMFASLL
KQDMAFFNER KTGELMSRLA SDVSSVRSII SDSIPHMIIQ IATIGGTLIM LFIISWKLSL
VVLCPLPILL VFSKFYGGYI EVISVKVQDA LADAATHAAE TLFNMKTVRW FSAEEREVAK
FSKLISVSYK IALKMTIWNG IYSSTSGIFE QLSVFILLWY GSSLVSNGDL TPSMLIAFNL
FLPFITGAVT QVASLYTTYK SYKGSSYRFF EIMQRVPDIQ GEGGITRTKV RGDIQFNKVS
FAYSSNPDQL VLEKIDIKFE PGTITALIGP SGGGKSTMLS LIGRLYNIDG GSITLDGTNI
KDFNVPNLHE HISIVNQEPS LFSGSIAENI MFGKPTATRS EIIEACKQAN AHDFITAMPE
GYDTLIGERG TALSGGQKQR IAIARTIIKN PTVLLLDETT SELDVESEKL VQDSIDKLVV
GRTVIIVAHR LTTILTADII AVVSDSTISE MGTPEELLAK KGMFYDFVQI QYGKQGEELD
IQLPSNSRNT RNADKLRNRS ETIKQIAKIN NIIPIHRPQR GDDDNEDDEN NSGQGSSRSP
PPMWRQAKKN ANVNKSMLLT RRNTHVQHQS SSGGWQKGNV DDKLQRVLQK SRKKGFMNNQ
DHKDIKATLV LY
