ID J3QT58_HUMAN Unreviewed; 182 AA. AC J3QT58; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 02-OCT-2024, entry version 77. DE SubName: Full=Carboxypeptidase A2 {ECO:0000313|EMBL:ALQ33449.1, ECO:0000313|Ensembl:ENSP00000395582.1}; GN Name=CPA2 {ECO:0000313|EMBL:ALQ33449.1, GN ECO:0000313|Ensembl:ENSP00000395582.1}; 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 {ECO:0000313|Ensembl:ENSP00000395582.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000395582.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11237011; DOI=10.1038/35057062; RG International Human Genome Sequencing Consortium; RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K., RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P., RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J., RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C., RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J., RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C., RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I., RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S., RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S., RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S., RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A., RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R., RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A., RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W., RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T., RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E., RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B., RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L., RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y., RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C., RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W., RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P., RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M., RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A., RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A., RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M., RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R., RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A., RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J., RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N., RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L., RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G., RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R., RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G., RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W., RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J., RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M., RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J., RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E., RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J., RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F., RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A., RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K., RA Shizuya H., Choi S., Chen Y.J.; RT "Initial sequencing and analysis of the human genome."; RL Nature 409:860-921(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000395582.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., RA Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., RA Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., RA Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., RA Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., RA Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] {ECO:0000313|Ensembl:ENSP00000395582.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496913; DOI=10.1038/nature03001; RG International Human Genome Sequencing Consortium; RT "Finishing the euchromatic sequence of the human genome."; RL Nature 431:931-945(2004). RN [4] {ECO:0000313|EMBL:ALQ33449.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26871637; DOI=10.1016/j.cell.2016.01.029; RA Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T., RA Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K., RA Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q., RA Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D., RA Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J., RA Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P., RA Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.; RT "Widespread Expansion of Protein Interaction Capabilities by Alternative RT Splicing."; RL Cell 164:805-817(2016). RN [5] {ECO:0000313|Ensembl:ENSP00000395582.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: Belongs to the peptidase M14 family. CC {ECO:0000256|ARBA:ARBA00005988}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC024085; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KU177991; ALQ33449.1; -; mRNA. DR Ensembl; ENST00000416698.1; ENSP00000395582.1; ENSG00000158516.12. DR UCSC; uc064hyv.1; human. DR HGNC; HGNC:2297; CPA2. DR VEuPathDB; HostDB:ENSG00000158516; -. DR GeneTree; ENSGT00940000160121; -. DR HOGENOM; CLU_019326_5_0_1; -. DR ChiTaRS; CPA2; human. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000158516; Expressed in body of pancreas and 102 other cell types or tissues. DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR036990; M14A-like_propep. DR InterPro; IPR003146; M14A_act_pep. DR InterPro; IPR000834; Peptidase_M14. DR PANTHER; PTHR11705:SF71; CARBOXYPEPTIDASE A2; 1. DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1. DR Pfam; PF00246; Peptidase_M14; 1. DR Pfam; PF02244; Propep_M14; 1. DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 1: Evidence at protein level; KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645, KW ECO:0000313|EMBL:ALQ33449.1}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Proteomics identification {ECO:0007829|PeptideAtlas:J3QT58, KW ECO:0007829|ProteomicsDB:J3QT58}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..182 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014579734" FT DOMAIN 27..100 FT /note="Carboxypeptidase activation peptide" FT /evidence="ECO:0000259|Pfam:PF02244" FT DOMAIN 127..166 FT /note="Peptidase M14 carboxypeptidase A" FT /evidence="ECO:0000259|Pfam:PF00246" FT REGION 159..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 182 AA; 20832 MW; 6F707DB75CF57A7E CRC64; MRLILFFGAL FGHIYCLETF VGDQVLEIVP SNEEQIKNLL QLEAQEHLQL DFWKSPTTPG ETAHVRVPFV NVQAVKVFLE SQGIAYSIMI EDVQVLLDKE NEEMLFNRRR ERSGNFNFGA YHTLEEISQE MDNLVAEHPG LVSKVNIGSS FENRPMNVLK KSSGRMQKDD GQLNPKPQRQ TP //