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VIP1_BOVIN
ID   VIP1_BOVIN              Reviewed;        1477 AA.
AC   A7Z050;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 {ECO:0000250|UniProtKB:Q6PFW1};
DE            EC=2.7.4.24 {ECO:0000250|UniProtKB:Q6PFW1};
DE   AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
DE   AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
DE   AltName: Full=InsP6 and PP-IP5 kinase 1;
GN   Name=PPIP5K1 {ECO:0000250|UniProtKB:Q6PFW1}; Synonyms=HISPPD2A, VIP1;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC       group-containing inositol pyrophosphates diphosphoinositol
CC       pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC       tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC       respectively called InsP7 and InsP8, regulate a variety of cellular
CC       processes, including apoptosis, vesicle trafficking, cytoskeletal
CC       dynamics, exocytosis, insulin signaling and neutrophil activation.
CC       Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to
CC       produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC       (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1,
CC       produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when
CC       cells are exposed to hyperosmotic stress.
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-myo-
CC         inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC         ChEBI:CHEBI:456216; EC=2.7.4.24;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC         + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC         + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane
CC       upon activation of the PtdIns 3-kinase pathway.
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- DOMAIN: The C-terminal acid phosphatase-like domain binds
CC       PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase
CC       domain of histidine acid phosphatases, it has no phosphatase activity.
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC153248; AAI53249.1; -; mRNA.
DR   RefSeq; NP_001098824.1; NM_001105354.1.
DR   RefSeq; XP_005222243.1; XM_005222186.3.
DR   AlphaFoldDB; A7Z050; -.
DR   SMR; A7Z050; -.
DR   STRING; 9913.ENSBTAP00000018635; -.
DR   PaxDb; A7Z050; -.
DR   PRIDE; A7Z050; -.
DR   Ensembl; ENSBTAT00000077582; ENSBTAP00000069005; ENSBTAG00000014005.
DR   Ensembl; ENSBTAT00000084525; ENSBTAP00000071334; ENSBTAG00000014005.
DR   GeneID; 510684; -.
DR   KEGG; bta:510684; -.
DR   CTD; 9677; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014005; -.
DR   VGNC; VGNC:33206; PPIP5K1.
DR   eggNOG; KOG1057; Eukaryota.
DR   GeneTree; ENSGT00390000009048; -.
DR   HOGENOM; CLU_000914_0_0_1; -.
DR   InParanoid; A7Z050; -.
DR   OrthoDB; 93740at2759; -.
DR   TreeFam; TF313594; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000014005; Expressed in retina and 102 other tissues.
DR   ExpressionAtlas; A7Z050; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR037446; His_Pase_VIP1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR040557; VIP1_N.
DR   PANTHER; PTHR12750; PTHR12750; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..1477
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase 1"
FT                   /id="PRO_0000315687"
FT   REGION          27..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..453
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   REGION          910..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1131..1180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1190..1204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1226..1241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1442..1477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         224..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         248..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         257..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         332..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         337..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   MOD_RES         940
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         983
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         1033
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         1069
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         1141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2ARP1"
FT   MOD_RES         1148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
SQ   SEQUENCE   1477 AA;  163665 MW;  DF692A0B30BB1EB4 CRC64;
     MWSLPASEGE SATAHFFLGA GDEGLGTRGL GMRPEESDSE LLEDEEDEVP PEPQIIVGIC
     AMTKKSKSKP MTQILERLCR FDYLTVIILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
     AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG
     EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
     KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM
     EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
     LAPQFQIPWS IPMEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFS
     LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY
     GHFSGINRKV QLTYYPHGVK ASNEGQDTQR EALAPSLLLV LKWGGELTPA GRVQAEELGR
     AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
     TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY NQLAPTGSTS
     LLSSMAVIQN PVKVCDQVFD LIENLTHQIR ERMQDPKSVD LQLYHSETLE LMLQRWSKLE
     RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
     EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH
     VHSLLSVFRY GGLLDETKDT QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH
     VELHFSPGVK GVEEEGSAPT GCGFRPASSE NEERKADQGS VEDLCPGKAS DEPDRALQTS
     PLPSEGPGLP KRSPLIRNRK AGSMEVLSET SSSRPGGHRL FSSSRPPTEM KQSGLGSQCT
     GLFSTTVLGG SSSAPNLQDY ARSQGKKLPP ASLKHRDELL FVPAVKRFSV SFAKHPTNGF
     EGCSMVPTIY PLETLHNALS LRQVSEFLSR VCQRHTEAQA QASAALFDSM HSNQASDSPF
     SPPRTLHSPT LQLQQRSEKP PWYSSGPSST VSSAGPSSPT AVDGNCPFGF SDQPSVSSHV
     TEEYQGLGLL QEAPGSGAQE PPLEGQQEPF EQNQSPQEPP VETKKPCQEV AEEVSQPCQD
     IPEEVNQPCQ QVSDICQPCE ENHDDVDQTC QEVPQISQPC EDASQLYQKV SKEVCELCQN
     SEEVNQPCQG VPVEIGRLVH GFPVGVGGLA QEVLGEVGRP TQEIPEELSQ SCQEFSVDIG
     RLAQEASAIN LLSPDTPEVD NPPLEFPGEG ALQAQEVSEW VKQQQSYVVP ELIDQLSREE
     VPQVQCPPSN ANPQSQSLAP DQNAPLPPAT CDSSFSH
 
 
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