(data stored in ACNUC6163 zone)

HOVERGEN: B7Z880_HUMAN

ID   B7Z880_HUMAN            Unreviewed;      1123 AA.
AC   B7Z880;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-SEP-2009, entry version 5.
DE   SubName: Full=cDNA FLJ61731, highly similar to Probable phospholipid-transporting ATPase IB (EC 3.6.3.1);
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis;
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
RA   Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
RA   Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
RA   Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(In) = ADP +
CC       phosphate + phospholipid(Out).
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CC   -!- GENE_FAMILY: HBG050601 [ FAMILY / ALN / TREE ]
DR   EMBL; AK302980; BAH13866.1; -; mRNA.
DR   IPI; IPI00465166; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane m...; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-reg.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006539; ATPase_P-typ_Plipid-transl.
DR   PANTHER; PTHR11939; ATPase_P; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; B7Z880.
DR   SWISS-2DPAGE; B7Z880.
KW   ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Transmembrane.
SQ   SEQUENCE   1123 AA;  126279 MW;  D249397890D53661 CRC64;
     MSRATSVGDQ LEAPARTIYL NQPHLNKFRD NQISTAKYSV LTFLPRFLYE QIRRAANAFF
     LFIALLQQIP DVSPTGRYTT LVPLIIILTI AGIKEIVEDF KRHKADNAVN KKKTIVLRNG
     MWHTIMWKEV AVGDIVKVVN GQYLPADVVL LSSSEPQAMC YVETANLDGE TNLKIRQGLS
     HTADMQTREV LMKLSGTIEC EGPNRHLYDF TGNLNLDGKS LVALGPDQIL LRGTQLRNTQ
     WVFGIVVYTG HDTKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSAGALYWNR
     SHGEKNWYIK KMDTTSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA LFINWDTDMY
     YIGNDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF KKCSIAGVTY GHFPELAREP
     SSDDFCRMPP PCSDSCDFDD PRLLKNIEDR HPTAPCIQEF LTLLAVCHTV VPEKDGDNII
     YQASSPDEAA LVKGAKKLGF VFTARTPFSV IIEAMGQEQT FGILNVLEFS SDRKRMSVIV
     RTPSGRLRLY CKGADNVIFE RLSKDSKYME ETLCHLEYFA TEGLRTLCVA YADLSENEYE
     EWLKVYQEAS TILKDRAQRL EECYEIIEKN LLLLGATAIE DRLQAGVPET IATLLKAEIK
     IWVLTGDKQE TAINIGYSCR LVSQNMALIL LKEDSLDATR AAITQHCTDL GNLLGKENDV
     ALIIDGHTLK YALSFEVRRS FLDLALSCKA VICCRVSPLQ KSEIVDVVKK RVKAITLAIG
     DGANDVGMIQ TAHVGVGISG NEGMQATNNS DYAIAQFSYL EKLLLVHGAW SYNRVTKCIL
     YCFYKNVVLY IIEIFTALPP FTLGIFERSC TQESMLRFPQ LYKITQNGEG FNTKVFWGHC
     INALVHSLIL FWFPMKALEH DTVLTSGHAT DYLFVGNIVY TYVVVTVCLK AGLETTAWTK
     FSHLAVWGSM LTWLVFFGIY STIWPTIPIA PDMRGQATMV LSSAHFWLGL FLVPTACLIE
     DVAWRAAKHT CKKTLLEEVQ ELETKSRVLG KAVLRDSNGK RLNERDRLIK RLGRKTPPTL
     FRGSSLQQGV PHGYAFSQEE HGAVSQEEVI RAYDTTKKKS RKK
//

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