ACP7_HUMAN
ID ACP7_HUMAN Reviewed; 438 AA.
AC Q6ZNF0; B2RN68;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 127.
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:0000312|HGNC:HGNC:33781};
GN Synonyms=PAPL {ECO:0000303|PubMed:16793224},
GN PAPL1 {ECO:0000303|PubMed:16793224};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
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 [4]
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}.
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DR EMBL; AK131245; BAD18425.1; -; mRNA.
DR EMBL; AC011443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136721; AAI36722.1; -; mRNA.
DR EMBL; BC136722; AAI36723.1; -; mRNA.
DR CCDS; CCDS33018.1; -.
DR RefSeq; NP_001004318.2; NM_001004318.2.
DR RefSeq; XP_011525268.1; XM_011526966.2.
DR RefSeq; XP_016882296.1; XM_017026807.1.
DR AlphaFoldDB; Q6ZNF0; -.
DR SMR; Q6ZNF0; -.
DR BioGRID; 133739; 48.
DR IntAct; Q6ZNF0; 5.
DR STRING; 9606.ENSP00000327557; -.
DR DEPOD; ACP7; -.
DR GlyGen; Q6ZNF0; 3 sites.
DR iPTMnet; Q6ZNF0; -.
DR PhosphoSitePlus; Q6ZNF0; -.
DR BioMuta; ACP7; -.
DR DMDM; 269849643; -.
DR jPOST; Q6ZNF0; -.
DR MassIVE; Q6ZNF0; -.
DR PaxDb; Q6ZNF0; -.
DR PeptideAtlas; Q6ZNF0; -.
DR PRIDE; Q6ZNF0; -.
DR ProteomicsDB; 68020; -.
DR Antibodypedia; 48007; 14 antibodies from 6 providers.
DR DNASU; 390928; -.
DR Ensembl; ENST00000331256.10; ENSP00000327557.4; ENSG00000183760.11.
DR GeneID; 390928; -.
DR KEGG; hsa:390928; -.
DR MANE-Select; ENST00000331256.10; ENSP00000327557.4; NM_001004318.3; NP_001004318.2.
DR UCSC; uc002oki.4; human.
DR CTD; 390928; -.
DR DisGeNET; 390928; -.
DR GeneCards; ACP7; -.
DR HGNC; HGNC:33781; ACP7.
DR HPA; ENSG00000183760; Group enriched (brain, lymphoid tissue, skin).
DR MIM; 610490; gene.
DR neXtProt; NX_Q6ZNF0; -.
DR OpenTargets; ENSG00000183760; -.
DR VEuPathDB; HostDB:ENSG00000183760; -.
DR eggNOG; KOG1378; Eukaryota.
DR GeneTree; ENSGT00390000015485; -.
DR InParanoid; Q6ZNF0; -.
DR OMA; YADDWYL; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; Q6ZNF0; -.
DR PathwayCommons; Q6ZNF0; -.
DR SignaLink; Q6ZNF0; -.
DR BioGRID-ORCS; 390928; 12 hits in 1022 CRISPR screens.
DR ChiTaRS; ACP7; human.
DR GenomeRNAi; 390928; -.
DR Pharos; Q6ZNF0; Tdark.
DR PRO; PR:Q6ZNF0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6ZNF0; protein.
DR Bgee; ENSG00000183760; Expressed in cerebellum and 56 other tissues.
DR ExpressionAtlas; Q6ZNF0; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..438
FT /note="Acid phosphatase type 7"
FT /id="PRO_0000316824"
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"
FT CONFLICT 408
FT /note="I -> T (in Ref. 1; BAD18425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 50480 MW; 70C5109FAAB2DDC5 CRC64;
MHPLPGYWSC YCLLLLFSLG VQGSLGAPSA APEQVHLSYP GEPGSMTVTW TTWVPTRSEV
QFGLQPSGPL PLRAQGTFVP FVDGGILRRK LYIHRVTLRK LLPGVQYVYR CGSAQGWSRR
FRFRALKNGA HWSPRLAVFG DLGADNPKAV PRLRRDTQQG MYDAVLHVGD FAYNLDQDNA
RVGDRFMRLI EPVAASLPYM TCPGNHEERY NFSNYKARFS MPGDNEGLWY SWDLGPAHII
SFSTEVYFFL HYGRHLVQRQ FRWLESDLQK ANKNRAARPW IITMGHRPMY CSNADLDDCT
RHESKVRKGL QGKLYGLEDL FYKYGVDLQL WAHEHSYERL WPIYNYQVFN GSREMPYTNP
RGPVHIITGS AGCEERLTPF AVFPRPWSAV RVKEYGYTRL HILNGTHIHI QQVSDDQDGK
IVDDVWVVRP LFGRRMYL
