P15085 (CBPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carboxypeptidase A1
EC=3.4.17.1

Gene names

Name:	CPA1
Synonyms:	CPA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. Ref.2
Catalytic activity	Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. Ref.2
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Monomer. May form a complex with proelastase 2. Ref.12 Ref.13
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase M14 family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Traceable author statement Ref.9. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	metallocarboxypeptidase activity Traceable author statement Ref.9. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.8 Ref.9

Propeptide

17 – 110

94

Activation peptide

PRO_0000004345

Chain

111 – 419

309

Carboxypeptidase A1

PRO_0000004346

Regions

Region

179 – 182

4

Substrate binding

Region

254 – 255

2

Substrate binding

Region

307 – 308

2

Substrate binding

Sites

Active site

380

1

Nucleophile

Metal binding

179

1

Zinc; catalytic

Metal binding

182

1

Zinc; catalytic

Metal binding

306

1

Zinc; catalytic

Binding site

237

1

Substrate By similarity

Amino acid modifications

Disulfide bond

248 ↔ 271

Ref.12 Ref.13

Natural variations

Natural variant

208

1

A → T.
Corresponds to variant rs34474469 [ dbSNP | Ensembl ].

VAR_048593

Natural variant

276

1

H → R. Ref.4 Ref.7
Corresponds to variant rs17849959 [ dbSNP | Ensembl ].

VAR_054311

Experimental info

Sequence conflict

139 – 141

3

NPH → HPG AA sequence Ref.10

Secondary structure

1

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419

Helix Strand Turn

Details...

Turn

114 – 116

3

Helix

125 – 138

14

Turn

140 – 142

3

Beta strand

143 – 150

8

Beta strand

156 – 162

7

Beta strand

171 – 176

6

Helix

183 – 199

17

Turn

200 – 202

3

Helix

204 – 212

9

Beta strand

214 – 219

6

Helix

223 – 231

9

Helix

253 – 255

3

Beta strand

257 – 260

4

Beta strand

263 – 268

6

Helix

284 – 296

13

Beta strand

299 – 306

8

Beta strand

311 – 315

5

Helix

326 – 341

16

Turn

342 – 344

3

Beta strand

349 – 352

4

Helix

353 – 356

4

Helix

364 – 370

7

Beta strand

374 – 380

7

Beta strand

384 – 387

4

Helix

393 – 395

3

Helix

396 – 416

21

Sequences

	Sequence		Length	Mass (Da)
	P15085 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 439FAFFFAEE958B1	FASTA	419	47,140
	10 20 30 40 50 60 MRGLLVLSVL LGAVFGKEDF VGHQVLRISV ADEAQVQKVK ELEDLEHLQL DFWRGPAHPG 70 80 90 100 110 120 SPIDVRVPFP SIQAVKIFLE SHGISYETMI EDVQSLLDEE QEQMFAFRSR ARSTDTFNYA 130 140 150 160 170 180 TYHTLEEIYD FLDLLVAENP HLVSKIQIGN TYEGRPIYVL KFSTGGSKRP AIWIDTGIHS 190 200 210 220 230 240 REWVTQASGV WFAKKITQDY GQDAAFTAIL DTLDIFLEIV TNPDGFAFTH STNRMWRKTR 250 260 270 280 290 300 SHTAGSLCIG VDPNRNWDAG FGLSGASSNP CSETYHGKFA NSEVEVKSIV DFVKDHGNIK 310 320 330 340 350 360 AFISIHSYSQ LLMYPYGYKT EPVPDQDELD QLSKAAVTAL ASLYGTKFNY GSIIKAIYQA 370 380 390 400 410 SGSTIDWTYS QGIKYSFTFE LRDTGRYGFL LPASQIIPTA KETWLALLTI MEHTLNHPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1." Catasus L., Villegas V., Pascual R., Aviles F.X., Wicker-Planquart C., Puigserver A. Biochem. J. 287:299-303(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreas.
[2]	"Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2." Laethem R.M., Blumenkopf T.A., Cory M., Elwell L., Moxham C.P., Ray P.H., Walton L.M., Smith G.K. Arch. Biochem. Biophys. 332:8-18(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-276.
[5]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-276. Tissue: Pancreas.
[8]	"Further studies on the human pancreatic binary complexes involving procarboxypeptidase A." Moulard M., Michon T., Kerfelec B., Chapus C. FEBS Lett. 261:179-183(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-43 AND 114-135, INTERACTION WITH PROELASTASE 2.
[9]	"Purification and properties of five different forms of human procarboxypeptidases." Pascual R., Burgos F.J., Salva M., Soriano F., Mendez E., Aviles F.X. Eur. J. Biochem. 179:609-616(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-42.
[10]	"Separation of human pancreatic carboxypeptidase A isoenzymes by high performance liquid chromatography." Linder D., Linder M., Schade H., Sziegoleit A. Biomed. Chromatogr. 7:143-145(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 113-143. Tissue: Pancreas.
[11]	"Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter." Stewart E.A., Craik C.S., Hake L., Bowcock A.M. Am. J. Hum. Genet. 46:795-800(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 330-396.
[12]	"Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid)." Pallares I., Fernandez D., Comellas-Bigler M., Fernandez-Recio J., Ventura S., Aviles F.X., Bode W., Vendrell J. Acta Crystallogr. D 64:784-791(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 111-419 IN COMPLEX WITH POLYACRYLIC ACID AND ZINC IONS, SUBUNIT, DISULFIDE BOND.
[13]	"Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite." Sanglas L., Aviles F.X., Huber R., Gomis-Rueth F.X., Arolas J.L. Proc. Natl. Acad. Sci. U.S.A. 106:1743-1747(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-418 IN COMPLEX WITH ASCARIS CARBOXYPEPTIDASE INHIBITOR AND ZINC IONS, SUBUNIT, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67318 mRNA. Translation: CAA47732.1.
AK291493 mRNA. Translation: BAF84182.1.
BT007313 mRNA. Translation: AAP35977.1.
CH236950 Genomic DNA. Translation: EAL24089.1.
CH471070 Genomic DNA. Translation: EAW83763.1.
BC005279 mRNA. Translation: AAH05279.1.

IPI

IPI00009823.

PIR

S29127.

RefSeq

NP_001859.1. NM_001868.2.

UniGene

Hs.2879.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V77	X-ray	1.60	A/B	111-419	[»]
3FJU	X-ray	1.60	A	112-418	[»]

ProteinModelPortal

P15085.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48699N.

IntAct

P15085. 1 interaction.

STRING

9606.ENSP00000011292.

Protein family/group databases

MEROPS

M14.001.

PTM databases

PhosphoSite

P15085.

Polymorphism databases

DMDM

399196.

Proteomic databases

PaxDb

P15085.

PeptideAtlas

P15085.

PRIDE

P15085.

Protocols and materials databases

DNASU

1357.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000011292; ENSP00000011292; ENSG00000091704.
ENST00000579597; ENSP00000462830; ENSG00000264509.

GeneID

1357.

KEGG

hsa:1357.

UCSC

uc003vpx.3. human.

Organism-specific databases

CTD

1357.

GeneCards

GC07P130020.

HGNC

HGNC:2296. CPA1.

HPA

CAB025197.
HPA021836.

MIM

114850. gene.

neXtProt

NX_P15085.

PharmGKB

PA26816.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2866.

HOGENOM

HOG000252967.

HOVERGEN

HBG050815.

InParanoid

P15085.

KO

K08779.

OMA

MIEDVQS.

PhylomeDB

P15085.

Gene expression databases

ArrayExpress

P15085.

Bgee

P15085.

CleanEx

HS_CPA1.

Genevestigator

P15085.

GermOnline

ENSG00000091704. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.340. 1 hit.

InterPro

IPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]

Pfam

PF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]

PRINTS

PR00765. CRBOXYPTASEA.

SMART

SM00631. Zn_pept. 1 hit.
[Graphical view]

SUPFAM

SSF54897. Prot_inh_propept. 1 hit.

PROSITE

PS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P15085.

ChEMBL

CHEMBL2088.

ChiTaRS

CPA1. human.

EvolutionaryTrace

P15085.

GenomeRNAi

1357.

NextBio

5497.

SOURCE

Search...

Entry information

Entry name

CBPA1_HUMAN

Accession

Primary (citable) accession number: P15085
Secondary accession number(s): A4D1M1 , Q53XU0, Q9BS67, Q9UCF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.