(data stored in ACNUC7421 zone)

HOGENOM: SCHPO_3_PE287

ID   SCHPO_3_PE287                        STANDARD;      PRT;   1010 AA.
AC   SCHPO_3_PE287; P28876;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Plasma membrane ATPase 2; EC=3.6.3 6;AltName: Full=Proton
DE   pump 2; (SCHPO_3.PE287).
GN   Name=pma2; ORFNames=SPCC1020.01c, SPCC1393.01;
OS   SCHIZOSACCHAROMYCES POMBE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHPO_3.PE287.
CC       Schizosaccharomyces pombe chromosome III EF1 full sequence 1..2452883
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PMA2_SCHPO
CC   -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a
CC       hydrogen ion pump. The proton gradient it generates drives the
CC       active transport of nutrients by H(+)-symport. The resulting
CC       external acidification and/or internal alkinization may mediate
CC       growth responses.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- PTM: In addition to transient phosphorylation of the active site
CC       Asp residue, this protein, but not the product of the pma1 locus,
CC       is phosphorylated efficiently in isolated plasma membrane.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIIA subfamily.
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schizosaccharomyces_pombe;SPCC1020.01C;SPCC1020.01C-1;SPCC1020.01C-1.
DR   UniProtKB/Swiss-Prot; P28876; -.
DR   EMBL; M60471; AAA35325.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA18989.1; -; Genomic_DNA.
DR   PIR; A40945; PXZP2P.
DR   RefSeq; NP_587959.2; NM_001022950.1.
DR   ProteinModelPortal; P28876; -.
DR   SMR; P28876; 131-1003.
DR   STRING; P28876; -.
DR   EnsemblFungi; SPCC1020.01c-1; SPCC1020.01c-1; SPCC1020.01c.
DR   GeneID; 2539012; -.
DR   GenomeReviews; CU329672_GR; pma2.
DR   KEGG; spo:SPCC1020.01c; -.
DR   GeneDB_Spombe; SPCC1020.01c; -.
DR   eggNOG; fuNOG06156; -.
DR   GeneTree; EFGT00050000000742; -.
DR   OrthoDB; EOG47DDQ8; -.
DR   PhylomeDB; P28876; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002417-MON; -.
DR   ArrayExpress; P28876; -.
DR   GO; GO:0032153; C:cell division site; IDA:GeneDB_Spombe.
DR   GO; GO:0051286; C:cell tip; IDA:GeneDB_Spombe.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR000695; ATPase_P-typ_H-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006534; ATPase_P-typ_PM_proton-efflux.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 2.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; SCHPO_3.PE287; -.
KW   SPCC1020.01ccc7236820036002503210000011;
KW   P28876;
KW   ATP-binding; Cell membrane; Complete proteome; Hydrogen ion transport;
KW   Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   1010 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQRNNGEGRP EGMHRISRFL HGNPFKNNAS PQDDSTTRTE VYEEGGVEDS AVDYDNASGN
     AAPRLTAAPN THAQQANLQS GNTSITHETQ STSRGQEATT SPSLSASHEK PARPQTGEGS
     DNEDEDEDID ALIEDLYSQD QEEEQVEEEE SPGPAGAAKV VPEELLETDP KYGLTESEVE
     ERKKKYGLNQ MKEEKTNNIK KFLSFFVGPI QFVMELAAAL AAGLRDWVDF GVICALLLLN
     ATVGFVQEYQ AGSIVDELKK TMALKASVLR DGRVKEIEAS EIVPGDILHL DEGTICPADG
     RLITKDCFLQ VDQSAITGES LAVDKHQNDT MYSSSTVKRG EAFMVVTATA DSTFVGRAAS
     LVGAAGQSQG HFTEVLNGIG TILLVLVILT LLCIYTAAFY RSVRLAALLE YTLAITIIGV
     PVGLPAVVTT TMAVGAAYLA KKKAIVQKLS AIESLAGVEI LCSDKTGTLT KNRLSLGEPY
     CVEGVSPDDL MLTACLASSR KKKGLDAIDK AFLKALRNYP KAKDQLSKYK VLDFHPFDPV
     SKKITAYVEA PDGQRITCVK GAPLWVFKTV QDDHEVPEAI TDAYREQVND MASRGFRSLG
     VARKADGKQW EILGIMPCSD PPRHDTARTI HEAIGLGLRI KMLTGDAVGI AKETARQLGM
     GTNVYNAERL GLSGGGDMPG SEVNDFVEAA DGFAEVFPQH KYAVVDILQQ RGYLVAMTGD
     GVNDAPSLKK ADAGIAVEGA SDAARSAADI VFLAPGLSAI IDALKTSRQI FHRMYAYVVY
     RIALSLHLEI FLGLWLIIRN QLLNLELIVF IAIFADVATL AIAYDNAPYA MKPVKWNLPR
     LWGLATIVGI LLAIGTWIVN TTMIAQGQNR GIVQNFGVQD EVLFLQISLT ENWLIFITRC
     SGPFWSSFPS WQLSGAVLVV DILATLFCIF GWFKGGHQTS IVAVIRIWMY SFGIFCLIAG
     VYYILSESSS FDRWMHGKHK ERGTTRKLED FVMQLQRTST HHEAEGKVTS
//

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