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AT2B4_BOVIN
ID   AT2B4_BOVIN             Reviewed;        1207 AA.
AC   D3K0R6; D3K0R5; Q28059;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Plasma membrane calcium-transporting ATPase 4 {ECO:0000305};
DE            Short=PMCA4 {ECO:0000303|PubMed:21187283};
DE            EC=7.2.2.10 {ECO:0000250|UniProtKB:P23634};
GN   Name=ATP2B4 {ECO:0000250|UniProtKB:P23634};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   1-1175 (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=21187283; DOI=10.1074/jbc.m110.142836;
RA   Brandenburger T., Strehler E.E., Filoteo A.G., Caride A.J., Aumuller G.,
RA   Post H., Schwarz A., Wilhelm B.;
RT   "Switch of PMCA4 splice variants in bovine epididymis results in altered
RT   isoform expression during functional sperm maturation.";
RL   J. Biol. Chem. 286:7938-7946(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1137-1207 (ISOFORM 1).
RX   PubMed=2966397; DOI=10.1073/pnas.85.9.2914;
RA   Brandt P., Zurini M., Neve R.L., Rhoads R.E., Vanaman T.C.;
RT   "A C-terminal, calmodulin-like regulatory domain from the plasma membrane
RT   Ca2+-pumping ATPase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:2914-2918(1988).
CC   -!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme
CC       that catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium out of the cell (By similarity). By regulating sperm cells
CC       calcium homeostasis, may play a role in sperm motility (By similarity).
CC       {ECO:0000250|UniProtKB:P23634, ECO:0000250|UniProtKB:Q6Q477}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC         Evidence={ECO:0000250|UniProtKB:P23634};
CC   -!- ACTIVITY REGULATION: Activated by calcium/calmodulin.
CC       {ECO:0000250|UniProtKB:P23634}.
CC   -!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
CC       Interacts with calmodulin. {ECO:0000250|UniProtKB:P23634}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21187283};
CC       Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium,
CC       flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PMCA4b;
CC         IsoId=D3K0R6-1; Sequence=Displayed;
CC       Name=2; Synonyms=PMCA4a;
CC         IsoId=D3K0R6-2; Sequence=VSP_058016, VSP_058017;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is detected in brain, heart, liver,
CC       testis and epididymis. Isoform 2 is detected in brain (at protein
CC       level), heart, seminal vesicle and epididymis. There is a shift in
CC       expression from isoform 1 to isoform 2 along the length of the
CC       epididymis from caput to cauda (at protein level).
CC       {ECO:0000269|PubMed:21187283}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000305}.
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DR   EMBL; GU353069; ADB79572.1; -; mRNA.
DR   EMBL; GU353070; ADB79573.1; -; mRNA.
DR   EMBL; DAAA02041902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02041903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02041904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02041905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02041906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; J03649; AAA30393.1; -; mRNA.
DR   PIR; A31332; A31332.
DR   RefSeq; NP_001166065.1; NM_001172594.1.
DR   AlphaFoldDB; D3K0R6; -.
DR   SMR; D3K0R6; -.
DR   STRING; 9913.ENSBTAP00000018688; -.
DR   PaxDb; D3K0R6; -.
DR   PRIDE; D3K0R6; -.
DR   Ensembl; ENSBTAT00000071315; ENSBTAP00000057551; ENSBTAG00000014059. [D3K0R6-1]
DR   GeneID; 282146; -.
DR   KEGG; bta:282146; -.
DR   CTD; 493; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014059; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   GeneTree; ENSGT00940000154527; -.
DR   OrthoDB; 115892at2759; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000014059; Expressed in cardiac ventricle and 110 other tissues.
DR   ExpressionAtlas; D3K0R6; baseline.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR   GO; GO:0036487; F:nitric-oxide synthase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR   GO; GO:0030165; F:PDZ domain binding; IBA:GO_Central.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR   GO; GO:1901660; P:calcium ion export; IEA:Ensembl.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:1905145; P:cellular response to acetylcholine; ISS:UniProtKB.
DR   GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
DR   GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR   GO; GO:0140199; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:1900082; P:negative regulation of arginine catabolic process; IEA:Ensembl.
DR   GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR   GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR   GO; GO:1902548; P:negative regulation of cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
DR   GO; GO:1903249; P:negative regulation of citrulline biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR   GO; GO:0098736; P:negative regulation of the force of heart contraction; IEA:Ensembl.
DR   GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
DR   GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISS:UniProtKB.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW   Calmodulin-binding; Cell membrane; Cell projection; Cilium; Flagellum;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1207
FT                   /note="Plasma membrane calcium-transporting ATPase 4"
FT                   /id="PRO_0000435123"
FT   TOPO_DOM        1..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        122..147
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..843
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        844..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        865..871
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        872..892
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        893..918
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        919..939
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        940..957
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        958..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        978..994
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        995..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1016..1028
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1029..1049
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1050..1207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          294..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1086..1103
FT                   /note="Calmodulin-binding subdomain A"
FT                   /evidence="ECO:0000250|UniProtKB:P20020,
FT                   ECO:0000250|UniProtKB:P23634"
FT   REGION          1104..1113
FT                   /note="Calmodulin-binding subdomain B"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   REGION          1159..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        465
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P19156"
FT   BINDING         785
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         789
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23634"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23634"
FT   MOD_RES         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64542"
FT   MOD_RES         1102
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         300..311
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058016"
FT   VAR_SEQ         1105..1207
FT                   /note="KVVKAFHSSLHESIQKPKNQNSIHNFMTHPEFTIDEEGPRTPLLDEQEEEIF
FT                   EKVSKPGTKTSSLDGEVTPQTNKNNNTVDCCQVQIVASHSDSPLHSLETSV -> DVIN
FT                   TFQTGASFKGVLKRQTMGQHLDVKHVPSSSYVTVAPVKSPPTTSVAAAVSSPTLGNQSG
FT                   QSV (in isoform 2)"
FT                   /id="VSP_058017"
FT   CONFLICT        180
FT                   /note="L -> P (in Ref. 1; ADB79572)"
FT   CONFLICT        972
FT                   /note="L -> F (in Ref. 1; ADB79573)"
SQ   SEQUENCE   1207 AA;  133792 MW;  8811E298B456F5A2 CRC64;
     MTNPTEHTLP SNSILESREG EFGCTVMDLR KLMELRSSDA IDQINVHYGG VMNLCSRLKT
     NPVEGLSGNP ADLEKRKQVF GQNLIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
     FYRPPGGENE QCGLAVTSPE DEGEAEAGWI EGAAILFSVI IVVLVTAFND WSKEKQFRGL
     QNRIEKEQKF SVIRNGHIIQ LPVAEIVVGD IAQIKYGDLL PADGILIQGN DLKIDESSLT
     GESDHVKKSL ERDPMLLSGT HVMEGSGRMV VTAVGINSQT GIIFTLLGAS EGEEEEKKKK
     GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GIDSEEKEKK AAKLPKKEKS VLQGKLTRLA
     VQIGKAGLIM SAITVLILIL YFVIDNFVIQ RRPWLAECTP IYVQYFVKFF IIGVTVLVVA
     VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMSVVQA
     YIGDTRYHQI PSPDDLVPKV LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGNKTECALL
     GFVSDLKQDY HAVRSEVPEE KLYKVYTFNS VRKSMSTVIE KPGGGYRMYS KGASEIILRK
     CNRILDKKGE AVPFKNKDRD EMVRTVIEPM ACEGLRTLCI AYRDFNDGEP PWDNESEILT
     ELTCIAVVGI EDPVRPEVPE AIAKCKRAGI TVRMVTGDNI NTARAIATKC GIVTPGDDFL
     CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL RVLARSSPTD KHTLVKGIID STVGDQRQVV
     AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
     SKFLQFQLTV NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTDSLL
     KRRPYGRNKP LISRTMMKNI LGHAVYQLTV IFFLVFAGEK FFDIDSGRRA PLHSPPSQHY
     TIIFNTFVLM QLFNEINSRK IHGERNVFSG IFRNLIFCSV VLGTFISQII IVEFGGKPFS
     CTKLTLSQWF WCLFIGIGEL LWGQVISTIP TQSLKFLKEA GHGTTKEEIT KDAEGLDEID
     HAEMELRRGQ ILWFRGLNRI QTQIKVVKAF HSSLHESIQK PKNQNSIHNF MTHPEFTIDE
     EGPRTPLLDE QEEEIFEKVS KPGTKTSSLD GEVTPQTNKN NNTVDCCQVQ IVASHSDSPL
     HSLETSV
 
 
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