MAM1_SCHPO
ID MAM1_SCHPO Reviewed; 1336 AA.
AC P78966;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mating factor M secretion protein mam1;
DE AltName: Full=Multiple drug resistance protein homolog;
DE AltName: Full=P-glycoprotein;
GN Name=mam1; ORFNames=SPBC25B2.02c, SPBC2G5.09c;
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=9236781; DOI=10.1007/s004380050493;
RA Christensen P.U., Davey J., Nielsen O.;
RT "The Schizosaccharomyces pombe mam1 gene encodes an ABC transporter
RT mediating secretion of M-factor.";
RL Mol. Gen. Genet. 255:226-236(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 -!- FUNCTION: Required in S.pombe M (minus) cells for production of M-
CC factor pheromone. Involved in the transport of the farnesyl-derivation
CC of the M-factor pheromone.
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; U66305; AAC49779.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21260.1; -; Genomic_DNA.
DR PIR; T39978; T39978.
DR RefSeq; NP_001018819.2; NM_001021982.3.
DR AlphaFoldDB; P78966; -.
DR SMR; P78966; -.
DR BioGRID; 276933; 1.
DR STRING; 4896.SPBC25B2.02c.1; -.
DR TCDB; 3.A.1.206.2; the atp-binding cassette (abc) superfamily.
DR MaxQB; P78966; -.
DR PaxDb; P78966; -.
DR EnsemblFungi; SPBC25B2.02c.1; SPBC25B2.02c.1:pep; SPBC25B2.02c.
DR GeneID; 2540405; -.
DR KEGG; spo:SPBC25B2.02c; -.
DR PomBase; SPBC25B2.02c; mam1.
DR VEuPathDB; FungiDB:SPBC25B2.02c; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; P78966; -.
DR OMA; QNGEDMR; -.
DR PhylomeDB; P78966; -.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:P78966; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IMP:PomBase.
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:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0090539; P:peptide pheromone export by transmembrane transport; IMP:PomBase.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 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;
KW Pheromone response; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1336
FT /note="Mating factor M secretion protein mam1"
FT /id="PRO_0000093369"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 113..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 175..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 272..778
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 800..897
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 919..1336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 104..396
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 433..668
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 781..1066
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1099..1331
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1135..1142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
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 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1336 AA; 150887 MW; FF20666B8852CAB6 CRC64;
MHIHSDLSLP QFEHASIDPP SYSPQKSSFE EKKHNFSITN KSLETLRSQE SPCSTTFPVS
DRKDALLNIP TVVDDEFQHT EELAGVSSWS DFFYLFHFSD IPLIFGTLIF TCLSAALEPL
MTWTTGKVFD ALSQYATSQI TLGKMISLIN FNSLLITIFG LASCVFSFGV RFLWQYLSAI
AGKRARSLCF HVLSSKSSTF YSLTESKSGL VNSVDRCIQF YEKSISLPMF HIAENLAISL
SCLIISFRYS WSLTLVVLAS YPIIILVVGF INSFLSSAYE KDRKSSEKAA SILEKSISAI
QTVIFHSMQD TEYRYFADAC STSSKSFLRF SFLDAFQGGV SQFFLYSVFF QGLWFGNHLA
TTKRVNVGQV VTVFGSCLSV ASSLQQILPA IPDLIKGKFS SHFIKTLCES HDPIEAAKRS
AAKIKSISFE RGFRFDNVSF AYPSRDENLF SLINVSVFIP FGELVHIIGP SGSGKSTFIS
LLLRYFSPTY GNIYLDDFPL EEIDEHVLGS TITLVCQQPV IFDMTIRENI IMRNENASES
DFEEVCRLAL VDEFALTFDQ SYDTPCKEAS LSGGQQQRIA LARALLRDTE ILILDEPTSA
LDPITKNLVM DAIRAHRKGK TTLVITHDMS QINNDELVLV IDKGHLIQRC ARKELVLFED
FENNVSIDEK VLKEEADNPF ILPNEESLLE KYWINYNESF SQLSRESLFT SLESPFTDIE
SPTIVSRRKI VEQRKLRMEK ESFQETNVDQ TFHLFDDKEH ACSLTLIFKS IWKVKKLRWF
FLLGLLTSLI QGASVPIFAY VISKCLNLFM QIDPSIGVAF WSSMVLVVAA GSGASYFFSH
YIFSISAKIW CDHYRLLAVK VLFTQDQAWF DQIENYPLVL SKILVNNISD MRNMISSLIE
EVFIAFTMAI IGIAWSFATG WRLAAVLVAV SPILCLTSRM FSYIYVSTER MCQDVVISTT
SILHKTIVNL DTIKGYSVLS FFRENHKNSL RKSWEAFKRR AFWTSLGFAI NNSLLYFVRA
LLFYCSSIFI SKEFYTVEQM VQVLSLATFT LLMASTCIMS LPNVSASRIA TSRVLKLSSL
KPGNLHKSGY LKFPLVGKIE FDGVSFAYPD SERNHLALNN VSLSIEAREK VAIVGISGSG
KSTLVELLRK TYPSEDIYID GYPLTNIDTN WLLKKVAIVD QKPHLLGSTI LESLLYGVDR
DINSVMDALD KTYMTEVIQN LPNGLDTPLL EFSKNFSGGQ IQRLAFARAL LRNPRLLILD
ECTSALDSKS SLLLEKTIQN LSCTVLIITH QPSLMKLADR IIVMDSGIVK ESGSFDELMN
RHTHFWKLIH RGEWIE
