ID A0A0D2P070_GOSRA Unreviewed; 625 AA.
AC A0A0D2P070;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Purple acid phosphatase {ECO:0000256|RuleBase:RU361203};
DE EC=3.1.3.2 {ECO:0000256|RuleBase:RU361203};
GN ORFNames=B456_003G120700 {ECO:0000313|EMBL:KJB19833.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB19833.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB19833.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|RuleBase:RU361203};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000256|ARBA:ARBA00008723,
CC ECO:0000256|RuleBase:RU361203}.
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DR EMBL; CM001742; KJB19833.1; -; Genomic_DNA.
DR RefSeq; XP_012471138.1; XM_012615684.1.
DR RefSeq; XP_012471139.1; XM_012615685.1.
DR AlphaFoldDB; A0A0D2P070; -.
DR STRING; 29730.A0A0D2P070; -.
DR EnsemblPlants; KJB19833; KJB19833; B456_003G120700.
DR GeneID; 105788685; -.
DR Gramene; KJB19833; KJB19833; B456_003G120700.
DR KEGG; gra:105788685; -.
DR eggNOG; KOG1378; Eukaryota.
DR OMA; GPVQTTW; -.
DR OrthoDB; 456532at2759; -.
DR Proteomes; UP000032304; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR040974; Fn3_PAP.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR45778:SF44; PURPLE ACID PHOSPHATASE; 1.
DR PANTHER; PTHR45778; PURPLE ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF17808; fn3_PAP; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361203};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361203};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT CHAIN 31..625
FT /note="Purple acid phosphatase"
FT /evidence="ECO:0000256|RuleBase:RU361203"
FT /id="PRO_5005113166"
FT DOMAIN 62..180
FT /note="Purple acid phosphatase Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF17808"
FT DOMAIN 187..291
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 303..516
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 541..600
FT /note="Iron/zinc purple acid phosphatase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14008"
SQ SEQUENCE 625 AA; 69688 MW; C3FFA0BE573D253D CRC64;
MRSLSFLSME YLFLLMSILS QCLKFGSGTA AVVHAGNGDG VQPLSKIAIH KAVYALHENA
SVKAHPLVLG TKGGDSDWVT VEIECPKPSE DDWIAVFSPA NFSSSICQPS DDMEQFPRIC
SAPIKYKYAN DSDADYKKTG KSSLKFQLIN QREDFSFALF SGGLSDPKLV AVSNVISFAN
PKAPLYPRLS QGKSWNEMTV TWTSGYNVIE AVPFVEWGMK GESQTRSPAG TLTFHQNDMC
APPARTVGWR DPGFIHTSFL KDLWPSSVYT YKLGHKLVDG SYVWSKSYSF KSSPYPGQDS
LQRVVIFGDM GKAERDGSNE YSNYQPGSLN TTDQLIKDLK NIDIVFHIGD ITYANGYISQ
WDQFTSQVER IASTVPYMIA SGNHERDAPN SGSFYDGNDS GGECGVIAET MFYVPAENRA
KFWYSTDYGM FHFCIADSEH DWREGSEQYK FIEKCLASAD RRKQPWLIFV AHRVLGYSSS
YWKDASFGEP MGRESLQGLW QKYKVDIAFF GHIHNYERTC PVYQGQCMHV GKSHYSGTVN
GTIHVVVGGG GSHLSAFGPT QTSWSLYKDS DFGFVKLTAY NHSSLLFEYK KSSDGNVYDS
FTISRDYRDV LACVHDGCEP TTLGS
//
