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IMPA3_PIG
ID   IMPA3_PIG               Reviewed;         359 AA.
AC   F1RT67;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase {ECO:0000250|UniProtKB:Q80V26};
DE            Short=Golgi-resident PAP phosphatase {ECO:0000250|UniProtKB:Q80V26};
DE            Short=gPAPP {ECO:0000250|UniProtKB:Q80V26};
DE            EC=3.1.3.7 {ECO:0000250|UniProtKB:Q80V26};
DE   AltName: Full=3'(2'), 5'-bisphosphate nucleotidase 2;
DE   AltName: Full=Inositol monophosphatase domain-containing protein 1 {ECO:0000250|UniProtKB:Q80V26};
DE   AltName: Full=Myo-inositol monophosphatase A3 {ECO:0000250|UniProtKB:Q9NX62};
DE   AltName: Full=Phosphoadenosine phosphate 3'-nucleotidase {ECO:0000250|UniProtKB:Q80V26};
GN   Name=BPNT2; Synonyms=IMPA3, IMPAD1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-
CC       bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into
CC       adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in
CC       the formation of skeletal elements derived through endochondral
CC       ossification, possibly by clearing adenosine 3',5'-bisphosphate
CC       produced by Golgi sulfotransferases during glycosaminoglycan sulfation.
CC       Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or
CC       inositol phosphate (IP) substrates including I(1)P, I(1,4)P2,
CC       I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4.
CC       {ECO:0000250|UniProtKB:Q80V26}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC         Evidence={ECO:0000250|UniProtKB:Q80V26};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by lithium.
CC       {ECO:0000250|UniProtKB:Q80V26}.
CC   -!- PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26,
CC       ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}.
CC       Note=The catalytic core is predicted to reside within the Golgi lumen.
CC       {ECO:0000250|UniProtKB:Q9NX62}.
CC   -!- PTM: Contains N-linked glycan resistant to endoglycosydase H.
CC       {ECO:0000250|UniProtKB:Q9NX62}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU606955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001230561.1; NM_001243632.1.
DR   AlphaFoldDB; F1RT67; -.
DR   SMR; F1RT67; -.
DR   STRING; 9823.ENSSSCP00000006654; -.
DR   PaxDb; F1RT67; -.
DR   PeptideAtlas; F1RT67; -.
DR   PRIDE; F1RT67; -.
DR   Ensembl; ENSSSCT00000047997; ENSSSCP00000041117; ENSSSCG00000032846.
DR   Ensembl; ENSSSCT00015080712; ENSSSCP00015032630; ENSSSCG00015060402.
DR   Ensembl; ENSSSCT00025031505; ENSSSCP00025013224; ENSSSCG00025023245.
DR   Ensembl; ENSSSCT00030060210; ENSSSCP00030027568; ENSSSCG00030043195.
DR   Ensembl; ENSSSCT00035057333; ENSSSCP00035023038; ENSSSCG00035043150.
DR   Ensembl; ENSSSCT00040029549; ENSSSCP00040012361; ENSSSCG00040022038.
DR   Ensembl; ENSSSCT00045034080; ENSSSCP00045023650; ENSSSCG00045019989.
DR   Ensembl; ENSSSCT00050072099; ENSSSCP00050031002; ENSSSCG00050052949.
DR   Ensembl; ENSSSCT00055049864; ENSSSCP00055039839; ENSSSCG00055025239.
DR   Ensembl; ENSSSCT00060084515; ENSSSCP00060036599; ENSSSCG00060061949.
DR   Ensembl; ENSSSCT00065050314; ENSSSCP00065021793; ENSSSCG00065036885.
DR   Ensembl; ENSSSCT00070006115; ENSSSCP00070004996; ENSSSCG00070003183.
DR   GeneID; 100156925; -.
DR   KEGG; ssc:100156925; -.
DR   CTD; 54928; -.
DR   VGNC; VGNC:98737; BPNT2.
DR   eggNOG; KOG3853; Eukaryota.
DR   GeneTree; ENSGT00940000160216; -.
DR   HOGENOM; CLU_034742_0_0_1; -.
DR   InParanoid; F1RT67; -.
DR   OMA; GNSMSEY; -.
DR   OrthoDB; 1096950at2759; -.
DR   TreeFam; TF314300; -.
DR   Reactome; R-SSC-156584; Cytosolic sulfonation of small molecules.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Proteomes; UP000314985; Chromosome 4.
DR   Bgee; ENSSSCG00000032846; Expressed in medulla oblongata and 43 other tissues.
DR   ExpressionAtlas; F1RT67; baseline and differential.
DR   Genevisible; F1RT67; SS.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097657; F:3',5'-nucleotide bisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR   GO; GO:0030204; P:chondroitin sulfate metabolic process; IEA:Ensembl.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Glycoprotein; Golgi apparatus; Hydrolase; Magnesium; Membrane;
KW   Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="Golgi-resident adenosine 3',5'-bisphosphate 3'-
FT                   phosphatase"
FT                   /id="PRO_0000413414"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..359
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          86..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX62"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  38668 MW;  F9AD29BC8DAE3DD4 CRC64;
     MAPMGIRLSP LGVAVFCLLG LGVLYHLYSG FLAGRFSLFG MGGEPGGGAA GPGAAADGGT
     VDLREMLAVS VLAAVRGGDE VRRVRESNVL HEKSKGKTRE GADDKMTSGD VLSNRKMFYL
     LKTAFPNVQI NTEEHVDATD QEVILWDRKI PEDILKEIAT PQEVPAESVT VWIDPLDATQ
     EYTEDLRKYV TTMVCVAVNG KPVLGVIHKP FSEYTAWAMV DGGSNVKART SYNEKTPRIV
     VSRSHSGMVK QVALQTFGNQ TTIIPAGGAG YKVLALLDVP DKSQEKADLY IHVTYIKKWD
     ICAGNAILKA LGGHMTTLSG EEISYTGSDG IEGGLLASVR VDHQALVRKL PDLEKTGHK
 
 
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