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Database: UniProt
Entry: A0A3B5QKU7_XIPMA
LinkDB: A0A3B5QKU7_XIPMA
Original site: A0A3B5QKU7_XIPMA 
ID   A0A3B5QKU7_XIPMA        Unreviewed;       513 AA.
AC   A0A3B5QKU7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000256|ARBA:ARBA00040357};
DE   AltName: Full=Acid phosphatase-like protein 2 {ECO:0000256|ARBA:ARBA00041499};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000030860.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000030860.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000030860.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC         beta-D-2-O-P-Xyl]-L-seryl-[protein] + H2O = 3-O-(beta-D-GlcA-(1->3)-
CC         beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:56512, Rhea:RHEA-COMP:12573, Rhea:RHEA-
CC         COMP:14559, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:132093,
CC         ChEBI:CHEBI:140495; Evidence={ECO:0000256|ARBA:ARBA00036311};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   AlphaFoldDB; A0A3B5QKU7; -.
DR   Ensembl; ENSXMAT00000037738.1; ENSXMAP00000030860.1; ENSXMAG00000008348.2.
DR   GeneTree; ENSGT00390000016324; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF125; 2-PHOSPHOXYLOSE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..513
FT                   /note="2-phosphoxylose phosphatase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017185769"
FT   REGION          427..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  58007 MW;  ECE5C9794CBE62BA CRC64;
     MVSSVTGHFL FFFCIVSVNL IPTSPMLDEQ TVQAADGGFR GLQAKSRKRV FPVHHNQEPD
     PVFEAYSYCN TPNRTEQAWE GHSPVDYKLL SVHVMIRHGD RYPLYAIPKT RRPSIDCTLS
     ASRQPSHPLL TSFINHMGQG TKGHWEAQLG SISRLPNHSV CEMGELTQTG VVQHLRNGQL
     LQRAYKHHSL LPSDWSPRQV WMETTGKSRT LQSGMAFLYG FLPDFDWTKV TVRHQWSTLF
     CGSACECPAR SKYLEEEQRR QYRLRVADSN LERTYINMAR TLGVLTRQLR AANPIDSLLC
     HLCHGLSFPC VSSGDGGTGG CLTMAQFAVI RQQQLDDEVD RRRFGAYRKY AILAMYPYLN
     RTANKMEQVA RANEEGRQPR LGGEEVFTFS SGHDVTIAPL LSALGLEEAK FPRFAARIVF
     EMWKSPPTTQ GQAKNKAGKS ARSKSDQKDG DVFIRVLYNG EDVTFHTAFC HPSDRHTNQP
     LCPLKNFLTF VRKDIFSIVN ATSYKEACYK LSG
//
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