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   24-JAN-2024, entry version 131.
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}, Papl1
GN   {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   GlyCosmos; Q8BX37; 3 sites, No reported glycans.
DR   GlyGen; Q8BX37; 3 sites.
DR   iPTMnet; Q8BX37; -.
DR   PhosphoSitePlus; Q8BX37; -.
DR   PaxDb; 10090-ENSMUSP00000045437; -.
DR   ProteomicsDB; 285980; -.
DR   Antibodypedia; 48007; 24 antibodies from 6 providers.
DR   DNASU; 101744; -.
DR   Ensembl; ENSMUST00000159560.3; ENSMUSP00000147133.3; ENSMUSG00000037469.12.
DR   Ensembl; ENSMUST00000239470.2; ENSMUSP00000159320.2; ENSMUSG00000037469.12.
DR   GeneID; 101744; -.
DR   KEGG; mmu:101744; -.
DR   AGR; MGI:2142121; -.
DR   CTD; 390928; -.
DR   MGI; MGI:2142121; Acp7.
DR   VEuPathDB; HostDB:ENSMUSG00000037469; -.
DR   eggNOG; KOG1378; Eukaryota.
DR   GeneTree; ENSGT00390000015485; -.
DR   InParanoid; Q8BX37; -.
DR   OrthoDB; 203742at2759; -.
DR   BioGRID-ORCS; 101744; 1 hit in 77 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 44 other cell types or 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   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 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   PANTHER; PTHR45867:SF3; ACID PHOSPHATASE TYPE 7; 1.
DR   PANTHER; PTHR45867; PURPLE ACID PHOSPHATASE; 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   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
//