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VATB1_GOSHI
ID   VATB1_GOSHI             Reviewed;         488 AA.
AC   Q43432;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=V-type proton ATPase subunit B 1;
DE            Short=V-ATPase subunit B 1;
DE   AltName: Full=Vacuolar proton pump subunit B 1;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Acala SJ2; TISSUE=Ovule;
RX   PubMed=7972522; DOI=10.1104/pp.106.1.393;
RA   Wan C.Y., Wilkins T.A.;
RT   "Isolation of multiple cDNAs encoding the vacuolar H(+)-ATPase subunit B
RT   from developing cotton (Gossypium hirsutum L.) ovules.";
RL   Plant Physiol. 106:393-394(1994).
CC   -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC       vacuolar ATPase. V-ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC       attached to an integral membrane V0 proton pore complex (main
CC       component: the proteolipid protein).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; U07052; AAA57549.1; -; mRNA.
DR   RefSeq; NP_001313705.1; NM_001326776.1.
DR   AlphaFoldDB; Q43432; -.
DR   SMR; Q43432; -.
DR   PRIDE; Q43432; -.
DR   GeneID; 107890851; -.
DR   KEGG; ghi:107890851; -.
DR   Proteomes; UP000189702; Genome assembly.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022879; V-ATPase_su_B/beta.
DR   PANTHER; PTHR43389; PTHR43389; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..488
FT                   /note="V-type proton ATPase subunit B 1"
FT                   /id="PRO_0000144641"
SQ   SEQUENCE   488 AA;  54206 MW;  946ACFFD886ADB81 CRC64;
     MGMAENTNGM EEGTLEIGME YRTVSGVAGP LVILDKVKGP KYQEIVNIRL GDGTTRRGQV
     LEVDGEKAVV QVFEGTSGID NKYTTVQFTG EVLKTPVSLD MLGRIFNGSG KPIDNGPPIL
     PEAYLDISGS SINPSERTYP EEMIQTGIST IDVMNSIARG QKIPLFSAAG LPHNEIAAQI
     CRQAGLVKRL EKTGDLLEDG EEDNFAIVFA AMGVNMETAQ FFKRDFEENG SMERVTLFLN
     LANDPTIERI ITPRIALTTA EYLAYECGKH VLVILTDMSS YADALREVSA AREEVPGRRG
     YPGYMYTDLA TIYERAGRIE GRKGSITQIP ILTMPNDDIT HPTPDLTGYI TEGQIYIDRQ
     LHNRQIYPPI NVLPSLSRLM KSAIGEGMTR RDHADVSNQL YANYAIGKDV QAMKAVVGEE
     ALSSEDLLYL EFLDKFERKV VTQGAYDTRN IFQSLDLAWT LLRIFPRELL HRIPAKTHDQ
     YYSRDAGN
 
 
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