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Database: UniProt
Entry: V9L8X8_CALMI
LinkDB: V9L8X8_CALMI
Original site: V9L8X8_CALMI 
ID   V9L8X8_CALMI            Unreviewed;       101 AA.
AC   V9L8X8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
DE            EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520, ECO:0000256|RuleBase:RU000553};
GN   Name=acyp2 {ECO:0000313|Ensembl:ENSCMIP00000007060.1};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP08362.1};
RN   [1] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17185593; DOI=10.1126/science.1130708;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Ancient noncoding elements conserved in the human genome.";
RL   Science 314:1892-1892(2006).
RN   [2] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17407382;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Survey sequencing and comparative analysis of the elephant shark
RT   (Callorhinchus milii) genome.";
RL   PLoS Biol. 5:E101-E101(2007).
RN   [3] {ECO:0000313|EMBL:AFP08362.1, ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney {ECO:0000313|EMBL:AFP08362.1};
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
RN   [4] {ECO:0000313|Ensembl:ENSCMIP00000007060.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00520,
CC         ECO:0000256|RuleBase:RU000553};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|RuleBase:RU004168}.
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DR   EMBL; JW875845; AFP08362.1; -; mRNA.
DR   RefSeq; XP_007890607.1; XM_007892416.1.
DR   Ensembl; ENSCMIT00000007283.1; ENSCMIP00000007060.1; ENSCMIG00000003936.1.
DR   GeneID; 103177978; -.
DR   KEGG; cmk:103177978; -.
DR   GeneTree; ENSGT00390000011103; -.
DR   OrthoDB; 126107at2759; -.
DR   Proteomes; UP000314986; Unassembled WGS sequence.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR10029; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR10029:SF20; ACYLPHOSPHATASE-2; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520,
KW   ECO:0000256|RuleBase:RU000553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314986}.
FT   DOMAIN          11..101
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   101 AA;  11410 MW;  CFE2A62C7FAE742D CRC64;
     MSGAVAARMS SLDFEISGRV QGVCFRMYTE EQARKLGVVG WVRNTRQGTV EGQVQGTKDN
     VDSMKNWLSK VGSPSSRIDR ANFSNEKEIS KLEFKHFTTR Y
//
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