CBPA5_HUMAN
ID CBPA5_HUMAN Reviewed; 436 AA.
AC Q8WXQ8; G3V0G8; Q6ZNI6; Q86SE2; Q86XM3; Q8NA08;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Carboxypeptidase A5;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=CPA5;
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 [MRNA] (ISOFORM 1), AND VARIANTS SER-79; SER-336 AND
RP ASP-338.
RX PubMed=11920156; DOI=10.1038/sj.mp.4001004;
RA Bonora E., Bacchelli E., Levy E.R., Blasi F., Marlow A., Monaco A.P.,
RA Maestrini E.;
RT "Mutation screening and imprinting analysis of four candidate genes for
RT autism in the 7q32 region.";
RL Mol. Psychiatry 7:289-301(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Medulla oblongata;
RX PubMed=12676894; DOI=10.1136/jmg.40.4.249;
RA Bentley L., Nakabayashi K., Monk D., Beechey C., Peters J., Birjandi Z.,
RA Khayat F.E., Patel M., Preece M.A., Stanier P., Scherer S.W., Moore G.E.;
RT "The imprinted region on human chromosome 7q32 extends to the
RT carboxypeptidase A gene cluster: an imprinted candidate for Silver-Russell
RT syndrome.";
RL J. Med. Genet. 40:249-256(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
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 [4]
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.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-336
RP AND ASP-338.
RC TISSUE=Testis;
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 [7]
RP GENE STRUCTURE.
RX PubMed=11836249; DOI=10.1074/jbc.m112254200;
RA Wei S., Segura S., Vendrell J., Aviles F.X., Lanoue E., Day R., Feng Y.,
RA Fricker L.D.;
RT "Identification and characterization of three members of the human
RT metallocarboxypeptidase gene family.";
RL J. Biol. Chem. 277:14954-14964(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WXQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXQ8-2; Sequence=VSP_008806, VSP_008807;
CC Name=3;
CC IsoId=Q8WXQ8-3; Sequence=VSP_044866;
CC -!- TISSUE SPECIFICITY: Expression is very low or not detectable.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AF384667; AAL37611.1; -; mRNA.
DR EMBL; AY155229; AAO17155.1; -; mRNA.
DR EMBL; AY155230; AAO17156.1; -; mRNA.
DR EMBL; AK093288; BAC04122.1; -; mRNA.
DR EMBL; AK131191; BAD18389.1; -; mRNA.
DR EMBL; AC007938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471070; EAW83757.1; -; Genomic_DNA.
DR EMBL; BC039362; AAH39362.1; -; mRNA.
DR EMBL; BC042996; AAH42996.1; -; mRNA.
DR EMBL; BK000187; DAA00035.1; -; mRNA.
DR CCDS; CCDS47713.1; -. [Q8WXQ8-3]
DR CCDS; CCDS5819.1; -. [Q8WXQ8-1]
DR RefSeq; NP_001120913.1; NM_001127441.1. [Q8WXQ8-1]
DR RefSeq; NP_001120914.1; NM_001127442.1. [Q8WXQ8-3]
DR RefSeq; NP_001305152.1; NM_001318223.1. [Q8WXQ8-1]
DR RefSeq; NP_525124.3; NM_080385.4. [Q8WXQ8-1]
DR RefSeq; XP_005250767.1; XM_005250710.1. [Q8WXQ8-1]
DR RefSeq; XP_005250769.1; XM_005250712.1. [Q8WXQ8-1]
DR RefSeq; XP_011515000.1; XM_011516698.1. [Q8WXQ8-1]
DR RefSeq; XP_011515003.1; XM_011516701.1. [Q8WXQ8-1]
DR RefSeq; XP_011515004.1; XM_011516702.1. [Q8WXQ8-1]
DR RefSeq; XP_011515005.1; XM_011516703.1. [Q8WXQ8-1]
DR RefSeq; XP_011515006.1; XM_011516704.1. [Q8WXQ8-3]
DR AlphaFoldDB; Q8WXQ8; -.
DR SMR; Q8WXQ8; -.
DR BioGRID; 125066; 20.
DR IntAct; Q8WXQ8; 14.
DR MINT; Q8WXQ8; -.
DR STRING; 9606.ENSP00000420237; -.
DR MEROPS; M14.020; -.
DR iPTMnet; Q8WXQ8; -.
DR PhosphoSitePlus; Q8WXQ8; -.
DR BioMuta; CPA5; -.
DR DMDM; 38257690; -.
DR MassIVE; Q8WXQ8; -.
DR PaxDb; Q8WXQ8; -.
DR PeptideAtlas; Q8WXQ8; -.
DR PRIDE; Q8WXQ8; -.
DR ProteomicsDB; 32193; -.
DR ProteomicsDB; 75078; -. [Q8WXQ8-1]
DR ProteomicsDB; 75079; -. [Q8WXQ8-2]
DR TopDownProteomics; Q8WXQ8-1; -. [Q8WXQ8-1]
DR Antibodypedia; 32057; 97 antibodies from 24 providers.
DR DNASU; 93979; -.
DR Ensembl; ENST00000393213.7; ENSP00000376907.3; ENSG00000158525.16. [Q8WXQ8-1]
DR Ensembl; ENST00000431780.6; ENSP00000393045.2; ENSG00000158525.16. [Q8WXQ8-3]
DR Ensembl; ENST00000461828.5; ENSP00000418183.1; ENSG00000158525.16. [Q8WXQ8-1]
DR Ensembl; ENST00000466363.6; ENSP00000419025.2; ENSG00000158525.16. [Q8WXQ8-1]
DR Ensembl; ENST00000474905.6; ENSP00000417314.1; ENSG00000158525.16. [Q8WXQ8-1]
DR Ensembl; ENST00000485477.5; ENSP00000420237.1; ENSG00000158525.16. [Q8WXQ8-1]
DR GeneID; 93979; -.
DR KEGG; hsa:93979; -.
DR MANE-Select; ENST00000474905.6; ENSP00000417314.1; NM_080385.5; NP_525124.3.
DR UCSC; uc003vps.3; human. [Q8WXQ8-1]
DR CTD; 93979; -.
DR DisGeNET; 93979; -.
DR GeneCards; CPA5; -.
DR HGNC; HGNC:15722; CPA5.
DR HPA; ENSG00000158525; Tissue enriched (testis).
DR MIM; 609561; gene.
DR neXtProt; NX_Q8WXQ8; -.
DR OpenTargets; ENSG00000158525; -.
DR PharmGKB; PA26820; -.
DR VEuPathDB; HostDB:ENSG00000158525; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161666; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; Q8WXQ8; -.
DR OMA; AAWGQMN; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q8WXQ8; -.
DR TreeFam; TF317197; -.
DR PathwayCommons; Q8WXQ8; -.
DR SignaLink; Q8WXQ8; -.
DR BioGRID-ORCS; 93979; 10 hits in 1067 CRISPR screens.
DR GeneWiki; CPA5; -.
DR GenomeRNAi; 93979; -.
DR Pharos; Q8WXQ8; Tbio.
DR PRO; PR:Q8WXQ8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WXQ8; protein.
DR Bgee; ENSG00000158525; Expressed in right testis and 105 other tissues.
DR ExpressionAtlas; Q8WXQ8; baseline and differential.
DR Genevisible; Q8WXQ8; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR034248; CPA_M14_CPD.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carboxypeptidase; Cleavage on pair of basic residues;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..126
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004361"
FT CHAIN 127..436
FT /note="Carboxypeptidase A5"
FT /id="PRO_0000004362"
FT ACT_SITE 397
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 196..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 271..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 324..325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 265..288
FT /evidence="ECO:0000250|UniProtKB:Q96IY4"
FT VAR_SEQ 347..436
FT /note="YDLAKDAVEALYKVHGIEYIFGSISTTLYVASGITVDWAYDSGIKYAFSFEL
FT RDTGQYGFLLPATQIIPTAQETWMALRTIMEHTLNHPY -> MWPVGSPSTGPMTVASS
FT TPSALSSGTLGSMASCCRPHRSSPRPRRRGWRFGPSWSTP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044866"
FT VAR_SEQ 347..351
FT /note="YDLAK -> VRLAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008806"
FT VAR_SEQ 352..436
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008807"
FT VARIANT 79
FT /note="P -> S (in dbSNP:rs17388190)"
FT /evidence="ECO:0000269|PubMed:11920156"
FT /id="VAR_017191"
FT VARIANT 336
FT /note="L -> S (in dbSNP:rs11761888)"
FT /evidence="ECO:0000269|PubMed:11920156,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_017192"
FT VARIANT 338
FT /note="E -> D (in dbSNP:rs17854248)"
FT /evidence="ECO:0000269|PubMed:11920156,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_017193"
FT VARIANT 378
FT /note="S -> G (in dbSNP:rs11765961)"
FT /id="VAR_048596"
FT CONFLICT 108
FT /note="K -> R (in Ref. 3; BAC04122)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> G (in Ref. 6; AAH39362)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="H -> R (in Ref. 3; BAD18389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49036 MW; A6EB4FFDE72F355A CRC64;
MQGTPGGGTR PGPSPVDRRT LLVFSFILAA ALGQMNFTGD QVLRVLAKDE KQLSLLGDLE
GLKPQKVDFW RGPARPSLPV DMRVPFSELK DIKAYLESHG LAYSIMIKDI QVLLDEERQA
MAKSRRLERS TNSFSYSSYH TLEEIYSWID NFVMEHSDIV SKIQIGNSFE NQSILVLKFS
TGGSRHPAIW IDTGIHSREW ITHATGIWTA NKIVSDYGKD RVLTDILNAM DIFIELVTNP
DGFAFTHSMN RLWRKNKSIR PGIFCIGVDL NRNWKSGFGG NGSNSNPCSE TYHGPSPQSE
PEVAAIVNFI TAHGNFKALI SIHSYSQMLM YPYGRLLEPV SNQRELYDLA KDAVEALYKV
HGIEYIFGSI STTLYVASGI TVDWAYDSGI KYAFSFELRD TGQYGFLLPA TQIIPTAQET
WMALRTIMEH TLNHPY
