CBPA4_MOUSE
ID CBPA4_MOUSE Reviewed; 420 AA.
AC Q6P8K8; Q8BMK6; Q9CTE6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Carboxypeptidase A4;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=Cpa4;
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; TISSUE=Embryo, and Head;
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=Pituitary;
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).
CC -!- FUNCTION: Metalloprotease that could be involved in the histone
CC hyperacetylation pathway. Releases a C-terminal amino acid, with
CC preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val. {ECO:0000250}.
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 -!- SUBUNIT: Interacts with LXN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AK003823; BAB23019.1; -; mRNA.
DR EMBL; AK030705; BAC27090.1; -; mRNA.
DR EMBL; BC061206; AAH61206.1; -; mRNA.
DR CCDS; CCDS19975.1; -.
DR RefSeq; NP_082202.1; NM_027926.3.
DR AlphaFoldDB; Q6P8K8; -.
DR SMR; Q6P8K8; -.
DR STRING; 10090.ENSMUSP00000048558; -.
DR MEROPS; M14.017; -.
DR GlyGen; Q6P8K8; 1 site.
DR iPTMnet; Q6P8K8; -.
DR PhosphoSitePlus; Q6P8K8; -.
DR MaxQB; Q6P8K8; -.
DR PaxDb; Q6P8K8; -.
DR PeptideAtlas; Q6P8K8; -.
DR PRIDE; Q6P8K8; -.
DR ProteomicsDB; 265283; -.
DR Antibodypedia; 17950; 90 antibodies from 26 providers.
DR DNASU; 71791; -.
DR Ensembl; ENSMUST00000049251; ENSMUSP00000048558; ENSMUSG00000039070.
DR GeneID; 71791; -.
DR KEGG; mmu:71791; -.
DR UCSC; uc009bfo.1; mouse.
DR CTD; 51200; -.
DR MGI; MGI:1919041; Cpa4.
DR VEuPathDB; HostDB:ENSMUSG00000039070; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161774; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; Q6P8K8; -.
DR OMA; QQNEGQE; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q6P8K8; -.
DR TreeFam; TF317197; -.
DR BioGRID-ORCS; 71791; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cpa4; mouse.
DR PRO; PR:Q6P8K8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6P8K8; protein.
DR Bgee; ENSMUSG00000039070; Expressed in lip and 30 other tissues.
DR Genevisible; Q6P8K8; MM.
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 Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004359"
FT CHAIN 114..420
FT /note="Carboxypeptidase A4"
FT /id="PRO_0000004360"
FT ACT_SITE 381
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 180..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 255..256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 308..309
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..272
FT /evidence="ECO:0000250|UniProtKB:Q96IY4"
FT CONFLICT 210
FT /note="I -> V (in Ref. 2; AAH61206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 47339 MW; 4A7B56A137C4B123 CRC64;
MKWLLFFGAL IGAGICGRDK FFGDQVFRIN VRNGDEIRKL TELVNSDHLK LSVWKSPSTF
DRPVDILVPS VSLLPVKSFL KSQGLDYSVT IEDLQALLDN EDEEMQHNEG IERSGDFNYG
AYHPLEAIYH EMDSIATDFP ELVSRVKIGE TFEKRPMYVL KFSTGGGKKR PAIWLNAGIH
AREWISQATA IWTARKIVTD YKKDPAITSI LKKVDIFLLP VANPDGYVYT QSQNRLWRKT
RSRNPGSRCV GADPNRNWNA SFAGEGTSDN PCSEVYHGSH PNSEVEVKSV VDFIQKHGNF
KCFIDLHSYS QLLMYPYGYT VKKAPDAEEL DDVARNAAQA LASLSGTKYR VGPTCTTVYP
ASGSSVDWAY DNGIKYAFTF ELRDTGYYGF LLPASQIIPT AEETWLGLKT IMEHVRDHLY
