ACP7_MOUSE
ID ACP7_MOUSE Reviewed; 438 AA.
AC Q8BX37;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acid phosphatase type 7 {ECO:0000305};
DE EC=3.1.3.2;
DE AltName: Full=Purple acid phosphatase long form {ECO:0000303|PubMed:16793224};
DE Flags: Precursor;
GN Name=Acp7 {ECO:0000250|UniProtKB:Q6ZNF0};
GN Synonyms=Papl {ECO:0000303|PubMed:16793224},
GN Papl1 {ECO:0000303|PubMed:16793224};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION.
RX PubMed=16793224; DOI=10.1016/j.gene.2006.02.031;
RA Flanagan J.U., Cassady A.I., Schenk G., Guddat L.W., Hume D.A.;
RT "Identification and molecular modeling of a novel, plant-like, human purple
RT acid phosphatase.";
RL Gene 377:12-20(2006).
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94908.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI32376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC33559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK049131; BAC33559.1; ALT_INIT; mRNA.
DR EMBL; BC094908; AAH94908.1; ALT_INIT; mRNA.
DR EMBL; BC132375; AAI32376.1; ALT_INIT; mRNA.
DR CCDS; CCDS21050.2; -.
DR RefSeq; NP_780528.1; NM_175319.4.
DR RefSeq; XP_006539510.1; XM_006539447.3.
DR RefSeq; XP_006539512.1; XM_006539449.3.
DR RefSeq; XP_006539513.1; XM_006539450.1.
DR AlphaFoldDB; Q8BX37; -.
DR SMR; Q8BX37; -.
DR STRING; 10090.ENSMUSP00000045437; -.
DR GlyGen; Q8BX37; 3 sites.
DR iPTMnet; Q8BX37; -.
DR PhosphoSitePlus; Q8BX37; -.
DR PaxDb; Q8BX37; -.
DR PRIDE; Q8BX37; -.
DR ProteomicsDB; 285980; -.
DR Antibodypedia; 48007; 14 antibodies from 6 providers.
DR DNASU; 101744; -.
DR Ensembl; ENSMUST00000159560; ENSMUSP00000147133; ENSMUSG00000037469.
DR Ensembl; ENSMUST00000239470; ENSMUSP00000159320; ENSMUSG00000037469.
DR GeneID; 101744; -.
DR KEGG; mmu:101744; -.
DR CTD; 390928; -.
DR MGI; MGI:2142121; Acp7.
DR VEuPathDB; HostDB:ENSMUSG00000037469; -.
DR eggNOG; KOG1378; Eukaryota.
DR GeneTree; ENSGT00390000015485; -.
DR InParanoid; Q8BX37; -.
DR OrthoDB; 426430at2759; -.
DR BioGRID-ORCS; 101744; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Acp7; mouse.
DR PRO; PR:Q8BX37; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BX37; protein.
DR Bgee; ENSMUSG00000037469; Expressed in lip and 41 other tissues.
DR ExpressionAtlas; Q8BX37; baseline and differential.
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:UniProtKB-KW.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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 Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..438
FT /note="Acid phosphatase type 7"
FT /id="PRO_0000316825"
FT BINDING 141
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 438 AA; 50663 MW; A4DD79056E13C3B8 CRC64;
MSPFLGGWLF FCMLLPFSPG VQGAQEYPHV TPEQIHLSYL GEPGTMTVTW TTWAPARSEV
QFGSQLSGPL PFRAHGTARA FVDGGVLRRK LYIHRVTLRK LQPGAQYVYR CGSSQGWSRR
FRFTALKNGV HWSPRLAVFG DMGADNPKAL PRLRRDTQQG MFDAVLHVGD FAYNMDQDNA
RVGDRFMRLI EPVAASLPYM TCPGNHEQRY NFSNYKARFS MPGDNEGLWY SWDLGPAHII
SFSTEVYFFL HYGRHLIEKQ FRWLENDLQK ANKNRVARPW IITMGHRPMY CSNADLDDCT
RHESRVRKGL HGKLFGLEDL FHKYGVDLEF WAHEHSYERL WPIYNYQVFN GSLESPYTNP
RGPVHIITGS AGCEELLTPF VRKPRPWSAV RVKEYGYTRM HILNGTHMHI QQVSDDQDGK
IVDDVWVVRP LLGRMMYH
