ABC1_SCHPO
ID ABC1_SCHPO Reviewed; 1427 AA.
AC Q92337;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP-binding cassette transporter abc1;
GN Name=abc1; ORFNames=SPAC9E9.12c;
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 [GENOMIC DNA].
RX PubMed=9037770; DOI=10.1111/j.1574-6968.1997.tb10226.x;
RA Christensen P.U., Davis K., Nielsen O., Davey J.;
RT "Abc1: a new ABC transporter from the fission yeast Schizosaccharomyces
RT pombe.";
RL FEMS Microbiol. Lett. 147:97-102(1997).
RN [2]
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; Y09354; CAA70526.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16410.1; -; Genomic_DNA.
DR PIR; T39219; T39219.
DR RefSeq; NP_594585.1; NM_001020014.2.
DR AlphaFoldDB; Q92337; -.
DR SMR; Q92337; -.
DR BioGRID; 279094; 10.
DR STRING; 4896.SPAC9E9.12c.1; -.
DR MaxQB; Q92337; -.
DR PaxDb; Q92337; -.
DR PRIDE; Q92337; -.
DR EnsemblFungi; SPAC9E9.12c.1; SPAC9E9.12c.1:pep; SPAC9E9.12c.
DR GeneID; 2542640; -.
DR KEGG; spo:SPAC9E9.12c; -.
DR PomBase; SPAC9E9.12c; -.
DR VEuPathDB; FungiDB:SPAC9E9.12c; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_6_1; -.
DR InParanoid; Q92337; -.
DR OMA; KSAMTQE; -.
DR PhylomeDB; Q92337; -.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-9646399; Aggrephagy.
DR Reactome; R-SPO-9748787; Azathioprine ADME.
DR Reactome; R-SPO-9753281; Paracetamol ADME.
DR PRO; PR:Q92337; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C: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:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
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 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1427
FT /note="ATP-binding cassette transporter abc1"
FT /id="PRO_0000093303"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1086..1106
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1114..1134
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1223..1243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 262..549
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 579..807
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 862..1142
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1180..1422
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 614..621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1214..1221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1427 AA; 160612 MW; 94E5FD69AB0E96C3 CRC64;
MKMFQSFFSN YIDINFFRNA TLDQCLLLFY LSLFSLTNLF LIQKLFHANH TQHPLKKYFG
ETCLLEYIQI ILSIVSAALS FYLDTNAVWW AIRTITHLEI VGLNILSSLK YGSTLFSWIS
VANAFGLLLL RLISIYDFLT YSSWSFSVKG GSFLLLLPLA YNITLFLLVI IPLFFPRAWS
PTVKFSKVAR PSPEQTCSIF SLIFTYGWLN GIIWKSWKKP ITLTDVPALP DTECTQIWYS
RFAKNDRKSL MHTILLSLKS TILLMVFLSV LVSSTLFVTP LAIKKLLQYL QNPKSDEGNS
PFLWVFVLLI GPYLASVVKE LYVHVSRRFM LRIKAAITQM IYKKVLTSKT LFVAVDGSKI
NLDYVYNLLA KDVDNIGEMR EFIGIIARAP LEMGVSMYFL YQLLGWSAYV GLLLAILSSS
FPLLVASKIS RLTSIANTSS DERIRLTTEL LKSIKITKLF GWERPMLSRI QEKRSFEVNN
MYSLTLFDII FKSGMKIAPF ISMFITFAIY TKIMGHQLTP ATAFTSISMF GLLRYQFIWL
ASVSRQFIQF KVSLKRVDNF VYGNMVNDSS IESSDSFVFE NTSLSWSPTP STALFQLKNL
NFTIPRNQFT LVVGSTGSGK STLAMALLGE LHVISGKMTT PSISQRIAYV PQAAWLRNGT
IRSNILFGEP YDEERYFQII KACCLDSDLN SMNDGDLTYI HSNGSSLSGG QKQRVSLARA
LYSNAEVYIF DDIFSALDVS TSRKIYESCF LSTLLQHKTI ILFTHNVSLC LPIAENVIVL
KNSTAQLVSP DSIQELVPST FFSSNTKKDN IEEENLEPHS FSFDSTLASS SDNDEQRDFA
SNSSIVLLGL HYLKYFGSNK YILGSILLVM MSQVSLASIH FWIALWSGNS LFSLKLPSSF
SFLWGYAILL FIYFLMDLSR AITFAKGGRT ASENIHDILS ERVLYSPLHW FEKTAAGRIL
NRFSKDMYAT DNLLWASLEG MLLCVMAILI TMLNVTLVMP IFMVPAAFVS LLVYLHGYAY
SKAQKQLTSL QSSRTSPVFT MLGETLGGIT VIRAFKKEKI FEHENMAFID DMIQPLYISF
AINRWLAIRT DGISGLVGFS TGLIALLRQN IPPGLVGFSL NSAIGFNISV LVFVRANNEI
LTYINNFRRL YEYMLLPSEK NESSCLTKPM NKEWPTLGHV SIKNLTVSYS IGQAAVLEDI
NLEILPKEKI AIVGRTGSGK STMGLTLLRF TMIMSGAVEV DGIDINSLDL EVLRQRISLI
PQDPVLISGT VRSNLDPFEE YGDGELNEIL KTASCESLVQ ASNKNSLDAF AIHLDTPVDS
GGVNFSSGQR QILALARALV RKSRIVILDE STASVDDTTD RRIQQMLRAA FKHATVLCIA
HRIKTIVDYD KVLVLDSGKT VEFGSPKSLY TQRRAFWKMC KESHISL
