YHYB_SCHPO
ID YHYB_SCHPO Reviewed; 766 AA.
AC O60159;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative anion/proton exchange transporter C19C7.11;
GN ORFNames=SPBC19C7.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Anion/proton exchange transporter involved in iron and copper
CC cation homeostasis. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi
CC apparatus membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Endosome membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA19579.2; -; Genomic_DNA.
DR PIR; T39817; T39817.
DR RefSeq; NP_596167.2; NM_001022087.2.
DR AlphaFoldDB; O60159; -.
DR SMR; O60159; -.
DR BioGRID; 277272; 3.
DR STRING; 4896.SPBC19C7.11.1; -.
DR iPTMnet; O60159; -.
DR MaxQB; O60159; -.
DR PaxDb; O60159; -.
DR PRIDE; O60159; -.
DR EnsemblFungi; SPBC19C7.11.1; SPBC19C7.11.1:pep; SPBC19C7.11.
DR GeneID; 2540750; -.
DR KEGG; spo:SPBC19C7.11; -.
DR PomBase; SPBC19C7.11; -.
DR VEuPathDB; FungiDB:SPBC19C7.11; -.
DR eggNOG; KOG0475; Eukaryota.
DR HOGENOM; CLU_003181_2_2_1; -.
DR InParanoid; O60159; -.
DR OMA; IMHLTIS; -.
DR Reactome; R-SPO-2672351; Stimuli-sensing channels.
DR PRO; PR:O60159; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015299; F:solute:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; ISO:PomBase.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:PomBase.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain; Cell membrane; Chloride; Chloride channel;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Ion channel;
KW Ion transport; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..766
FT /note="Putative anion/proton exchange transporter C19C7.11"
FT /id="PRO_0000310340"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..144
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..196
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..284
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..362
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..442
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..520
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 521..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 580..641
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 676..734
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 218
FT /note="Mediates proton transfer from the outer aqueous
FT phase to the interior of the protein; involved in linking
FT H(+) and Cl(-) transport"
FT /evidence="ECO:0000250"
FT SITE 275
FT /note="Mediates proton transfer from the protein to the
FT inner aqueous phase"
FT /evidence="ECO:0000250"
SQ SEQUENCE 766 AA; 85162 MW; 43733DCF104C0AF0 CRC64;
MSSQKRADSS SSFDQAERRS LDENERKKKY FFNREGSGID NFETDDRVNE IINEQNEENV
IDQSRWSKLW RIWNVGYSWF ILSIIGTTVG FAAYMLDIVT SWLSDIRRGY CTSHWYYNEK
FCCWYSETMG SSCTAWKPWT YKFSLNYLIY TAFALLFVLC AAIMVRDVAP LAAGSGISEI
KCIISGFLRD SFLSFRVMLV KCVGLPLAIA SGLSVGKEGP SVHLATTIGH NISKIFKYAR
EGSIRYRDIC VASAASGVAV AFGSPIGGVL FGIEEMSGGY DPKMIVYSFF CCLSAVGVLH
MLNPFRTGQV VLFEVRYSGS WHFFELLFFC FLGIFGGLYG EFVMRLFFLI QKLRKKYLSR
WGVLDAAFVT VITSLVSFLN PWLRLDMTLG MELLFQECKS SSSPELINLC DPSLRTKNTI
LLLIATFART IFVTFSYGAK VPAGIFVPSM AVGASFGYMI GLIAEMIYQR FPNSVLFLAC
HGSESCITPG TYALLGAAAS LSGIMHLTVT IVVIMFELTG ALNFILPTVL VVALANSIGN
MLGKTGIADR SIEINGLPLL EPEKSINSSN TINIPITEVM ASNLITIPSI GFTWRKLLGM
MEGYDFSGYP VVLDSRSNYL IGYLKKSSLK SSFEAAKLEP SFTFDQQLCF GKVDSVGDSK
SSKFGESDRI DLSAYMDVNP ISVLHTQSIA NVAVLFEVLS PSVIFIEKDG NLVGLISKKD
LLLASKYYQE DNDLVNPANR HRAVSTERIN DSYENIELKP LKLNIE
