ID A0A3L8SA41_CHLGU Unreviewed; 566 AA.
AC A0A3L8SA41;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000256|ARBA:ARBA00040357};
DE AltName: Full=Acid phosphatase-like protein 2 {ECO:0000256|ARBA:ARBA00041499};
GN ORFNames=DV515_00010045 {ECO:0000313|EMBL:RLV99099.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV99099.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV99099.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV99099.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV99099.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV99099.1}.
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DR EMBL; QUSF01000034; RLV99099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SA41; -.
DR STRING; 44316.ENSEGOP00005015912; -.
DR Proteomes; UP000276834; 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:UP000276834};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT REGION 24..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 64632 MW; 5343DE9F440106F2 CRC64;
MEKVPPKVSL NSSESQQCSL PPAVSMDGHG VAGQDPGQKL PSALSQGQGR QLLEQLVYVC
HMCVLAAANA SCIFFISLSW GEGDRLVPEN PITGQAQAFH CIRNICDWQQ KPQVHLIPVN
PVREDGLSPK SRKRIMPDLL TEPPAIDPVY EAQVYCNIPT VAERSMEGHA PHYFKLVSVQ
VLIRHGDRYP LYAIPKTKRP DIDCMLVPSR KPSHPQLEAF VKHMSKGSAA QMDGSLSSLP
HFPSHSLCEM GELTQTGVVQ HLRNGQLLRE IYINKHKLLP SDWTAKQLYL ETTGKSRTLQ
SALALLYTFL PDFDWKKINI RHQWSTIFCS GSCDCPMRNH YLEEEQRRQY SLRVKNNNLE
KIYVDMAKIV GIPTRQLRAS NPIDSLLCYF CHNVSFPCTK AGCIGMEHFK VIKRHQLEDE
RERQEKKLYF LYALLATHPL LNQTVNRLQR IAEGKKEEVF VLYSAHDVTL SPVLSALGIT
EARFPRFAAR LVFELWQDGK RPKEHFIRIL YNGADVTFQT SFCKDHYKRS SKPMCPLEKL
VNFVKRDMFL IFNSTNYYDA CHKRAL
//
