HST6_CANAW
ID HST6_CANAW Reviewed; 1323 AA.
AC P53706; C4YP26;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Alpha-factor-transporting ATPase;
DE EC=7.4.2.7;
DE AltName: Full=ATP-dependent permease HST6;
DE AltName: Full=STE6 homolog;
GN Name=HST6; ORFNames=CAWG_02961;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=9489670; DOI=10.1046/j.1365-2958.1998.00704.x;
RA Raymond M., Dignard D., Alarco A.-M., Mainville N., Magee B.B.,
RA Thomas D.Y.;
RT "A Ste6p/P-glycoprotein homologue from the asexual yeast Candida albicans
RT transports the a-factor mating pheromone in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 27:587-598(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [alpha-factor](in) + ATP + H2O = ADP + an [alpha-
CC factor](out) + H(+) + phosphate; Xref=Rhea:RHEA:10848, Rhea:RHEA-
CC COMP:11611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83228, ChEBI:CHEBI:456216; EC=7.4.2.7;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Alpha-factor
CC sex pheromone exporter (TC 3.A.1.206) family. {ECO:0000305}.
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DR EMBL; U13193; AAC49910.1; -; Genomic_DNA.
DR EMBL; CM000310; EEQ44685.1; -; Genomic_DNA.
DR PIR; T18214; T18214.
DR AlphaFoldDB; P53706; -.
DR SMR; P53706; -.
DR STRING; 5476.P53706; -.
DR EnsemblFungi; EEQ44685; EEQ44685; CAWG_02961.
DR VEuPathDB; FungiDB:CAWG_02961; -.
DR HOGENOM; CLU_000604_17_8_1; -.
DR OMA; QNGEDMR; -.
DR Proteomes; UP000001429; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000770; P:peptide pheromone export; IEA:InterPro.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR030246; Ste6/Hst6.
DR PANTHER; PTHR24223:SF372; PTHR24223:SF372; 2.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1323
FT /note="Alpha-factor-transporting ATPase"
FT /id="PRO_0000093371"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1120..1140
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1170..1190
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 45..337
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 373..609
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 678..969
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1035..1321
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1071..1078
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
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 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1097
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1323 AA; 148502 MW; 1DB102B209869C53 CRC64;
MFQEKSEKSS FPKRSSSLRS PSDSPAITSK NVFMFVNYSK DWPLILVGIL LMGGSAIATL
MNTYIYGEIM GKLSQFYLQD QSNHSFSQDI VKLCVGLIGI GCCKMILVWL GMFTWLKFGE
IQQSRARMQI YNKIINESQS WYDSKQNLIG QLTQINRCIE ELRSCNGEIL ASLMQTIVLI
LALLIMSFYQ SWSTTLIIMA SFPIMALCGW YFGKLTYKAQ QDENEVTSKA SKVFNWCYVN
PEMVRFFNSK NIELTKFKQL IEKSAQFYYK LSHAVAANTA VLKTLTLMMF VQGFWFGNYL
LSHKTITINQ LFTCFSSCLM LGQAVSGITE LLAILNTGHA AADKISGFLL QPPSKAKLLL
LHSKYPPFEI GSIYFKNVWF ESNSQNSVAI LQDVSFGILQ NQFNYVIGKS GSGKSTIAKL
LMRLYSVSRG TIEIDTVSID KLDPKYICQN ITLLEQNPVI FDDKTIAENI AIAIVDDYDS
LQAIPYYLIE QSAHFALLSD LDLNMKVNHL TLSGGQQQRI SIARAYLKNS PVLIMDESFS
ALDTETKQGL IEKVKKWRIG KTTIFITHEY KNILDDENVI ILDQGMIKNQ GQFKKMKNEE
IVQNYKSQGI ETSSYETTSQ SFSDNTKLPD GDYNYKTNPY ILKDLESQIK EDTDNEKLMG
VLAILRYCSS TINGKSLLGF GILLAIFQGV SSPVFSYCFS KLLSTSLDSS IGLNSTQKIL
QWSCISLSIA IFTGVTSYLS EFILNYCGEN WIVSLRQLTF FKLNNQDLSF FTGFDTNWSS
SEITALLMND TRDLRNLISQ FFPLLANLVS MTLIGIIWSI VSGWKLALVG ISFVPLVLLV
TVLYGKILES IENKYKCKVN NVELDLYRTI TTIRTIKIFN IQQYFETVFK EDLKVLNSIG
VYRALQTGIG FAISDLFSSI GQAIILFYGM KLISQFQYNY SQLLQVITLL SFTISNASIL
IHQLPEITRG QRAGTFIVKL LKDITSTMEV NDSCGVSSVR KRNSKSGSDS IGTIGPVKDN
QLFKKVTTDN DTLAISFNNV SFSYPNKLPY ILQLKSISLD VKKFTTIGIV GQSGSGKSTI
LKILFRLYDI KISPDSNTTK KYHDQTVKIF NQNLYLINSG LLCQTIAIVP QFPKFFSGTI
YDNLTYGINN TNSAGSNSSS SVSDSEIIKI LKLVNLHQFI VSLPQGLLTI MNDSDNDNDN
GNENENENEN GNTISTSSST SFTFSGGQLQ LLAIARALLR NPKILLLDEC TSNLDPITTK
IIINVIKSLH GKLTILFVTH DKELMRIADN LIVMKDGQIV EQGDFQQLIS NDGEFTKITK
TII
