CBPA6_MOUSE
ID CBPA6_MOUSE Reviewed; 438 AA.
AC Q5U901; Q8BVD0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Carboxypeptidase A6;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=Cpa6;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BLKS/J;
RX PubMed=15950771; DOI=10.1016/j.molbrainres.2005.02.026;
RA Fontenele-Neto J.D., Kalinina E., Feng Y., Fricker L.D.;
RT "Identification and distribution of mouse carboxypeptidase A-6.";
RL Brain Res. Mol. Brain Res. 137:132-142(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Colon;
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).
CC -!- FUNCTION: May be involved in the proteolytic inactivation of
CC enkephalins and neurotensin in some brain areas. May convert inactive
CC angiotensin I into the biologically active angiotensin II. Releases a
CC C-terminal amino acid, with preference for large hydrophobic C-terminal
CC amino acids and shows only very weak activity toward small amino acids
CC and histidine. {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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U901-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U901-2; Sequence=VSP_017081;
CC -!- TISSUE SPECIFICITY: In brain, highly expressed in the olfactory bulb
CC with lower levels in other regions including cerebral cortex,
CC hippocampus, hypothalamus, striatum and medulla. Within the olfactory
CC bulb, highest levels occur in the mitral and granular layers with lower
CC levels in the internal and external plexiform layers. Moderate levels
CC are found in the epididymis with low levels in colon and spleen. Not
CC detected in adrenal, liver, lung, ovary or testis. At embryonic day
CC 14.5, enriched in eye, ear, osteoblasts, stomach, skin, dorsal root
CC ganglia and throughout the CNS. {ECO:0000269|PubMed:15950771}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AY773477; AAV40814.1; -; mRNA.
DR EMBL; AK078883; BAC37442.1; -; mRNA.
DR CCDS; CCDS14819.1; -. [Q5U901-1]
DR RefSeq; NP_001276426.1; NM_001289497.1. [Q5U901-2]
DR RefSeq; NP_808502.2; NM_177834.4. [Q5U901-1]
DR AlphaFoldDB; Q5U901; -.
DR SMR; Q5U901; -.
DR STRING; 10090.ENSMUSP00000035435; -.
DR MEROPS; M14.018; -.
DR GlyGen; Q5U901; 4 sites.
DR PhosphoSitePlus; Q5U901; -.
DR PaxDb; Q5U901; -.
DR PRIDE; Q5U901; -.
DR ProteomicsDB; 265347; -. [Q5U901-1]
DR ProteomicsDB; 265348; -. [Q5U901-2]
DR Antibodypedia; 42507; 176 antibodies from 25 providers.
DR DNASU; 329093; -.
DR Ensembl; ENSMUST00000035577; ENSMUSP00000035435; ENSMUSG00000042501. [Q5U901-1]
DR GeneID; 329093; -.
DR KEGG; mmu:329093; -.
DR UCSC; uc007ahq.2; mouse. [Q5U901-1]
DR CTD; 57094; -.
DR MGI; MGI:3045348; Cpa6.
DR VEuPathDB; HostDB:ENSMUSG00000042501; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000159307; -.
DR HOGENOM; CLU_019326_0_3_1; -.
DR InParanoid; Q5U901; -.
DR OMA; HQHAREH; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q5U901; -.
DR TreeFam; TF317197; -.
DR BRENDA; 3.4.17.1; 3474.
DR BioGRID-ORCS; 329093; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Cpa6; mouse.
DR PRO; PR:Q5U901; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5U901; protein.
DR Bgee; ENSMUSG00000042501; Expressed in olfactory bulb layer and 64 other tissues.
DR ExpressionAtlas; Q5U901; baseline and differential.
DR Genevisible; Q5U901; 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 Gene3D; 3.30.70.340; -; 1.
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; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carboxypeptidase; Cleavage on pair of basic residues;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..129
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004367"
FT CHAIN 130..438
FT /note="Carboxypeptidase A6"
FT /id="PRO_0000004368"
FT ACT_SITE 399
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 197..200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 272..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 326..327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 266..289
FT /evidence="ECO:0000250|UniProtKB:Q96IY4"
FT VAR_SEQ 1..176
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017081"
SQ SEQUENCE 438 AA; 51143 MW; A6CB743AEFEFA18B CRC64;
MNFLGNPRSH TAAFLPVCWL LLNILKPGHC HSYDNRYAGD KVIRLIPKSE EEALALKNIY
HQLKVDLWQP SSISYVSEGT ITDVHISQNA SRTLLAFLQE THIYYKVLIE DLQKAVENEN
SLQTQRNRRS LSEYNYEVYH SLEDIQSWLH HLNQTQPGLV RVFSIGRSYE GRPLFIMQLG
RKSRAYKRAV WIDCGIHARE WIGPAFCQWF VREAILTYKT DPAMKKMLNH LYFYIMPVFN
VDGYHFSWTH DRFWRKTRSR DSKFRCRGVD ANRNWKVKWC DEGASAHPCD DTYCGPFPES
EPEVKAVANF LRKHRKRIRA YLSFHAYAQM LLYPYSYKYA TIPNFSCVEF AAHKAVKALR
SVHGIRYRHG PASQTLYVSS GNSMDWAYKN GIPYAFAFEL RDTGHFGFLL PEMLIKPTCT
ETMLAVKNIT MHLLKKCP
