P15086 (CBPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carboxypeptidase B
EC=3.4.17.2

Alternative name(s):
Pancreas-specific protein
Short name=PASP

Gene names

Name:	CPB1
Synonyms:	CPB, PCPB

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	417 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)

Catalytic activity	Preferential release of a C-terminal lysine or arginine amino acid.
Cofactor	Binds 1 zinc ion per subunit.
Subcellular location	Secreted.
Tissue specificity	Pancreas.
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 Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carboxypeptidase activity Traceable author statement Ref.1. Source: ProtInc metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro 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 – 15

15

Ref.1 Ref.6

Propeptide

16 – 110

95

Activation peptide

PRO_0000004371

Chain

111 – 417

307

Carboxypeptidase B

PRO_0000004372

Sites

Active site

378

1

Nucleophile By similarity

Metal binding

176

1

Zinc

Metal binding

179

1

Zinc

Metal binding

304

1

Zinc

Amino acid modifications

Disulfide bond

173 ↔ 186

Disulfide bond

245 ↔ 268

Disulfide bond

259 ↔ 273

Natural variations

Natural variant

208

1

D → N. Ref.2
Corresponds to variant rs1059502 [ dbSNP | Ensembl ].

VAR_048598

Experimental info

Sequence conflict

16

1

H → A AA sequence Ref.1

Sequence conflict

17

1

H → Q AA sequence Ref.1

Sequence conflict

37

1

H → Q AA sequence Ref.6

Sequence conflict

245

1

Missing in AAA66973. Ref.1

Secondary structure

1

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417

Helix Strand Turn

Details...

Helix

19 – 22

4

Beta strand

26 – 32

7

Helix

35 – 47

13

Beta strand

50 – 57

8

Helix

58 – 60

3

Beta strand

63 – 71

9

Helix

73 – 75

3

Helix

76 – 85

10

Beta strand

90 – 95

6

Helix

97 – 103

7

Beta strand

111 – 113

3

Helix

122 – 135

14

Turn

137 – 139

3

Beta strand

140 – 147

8

Beta strand

153 – 160

8

Beta strand

168 – 172

5

Helix

181 – 196

16

Turn

197 – 199

3

Helix

201 – 209

9

Beta strand

211 – 216

6

Helix

220 – 228

9

Helix

250 – 252

3

Beta strand

254 – 257

4

Beta strand

260 – 262

3

Helix

281 – 292

12

Turn

293 – 296

4

Beta strand

297 – 304

8

Beta strand

309 – 313

5

Beta strand

315 – 318

4

Helix

324 – 342

19

Beta strand

347 – 350

4

Helix

351 – 354

4

Helix

362 – 368

7

Beta strand

372 – 378

7

Beta strand

382 – 385

4

Helix

386 – 388

3

Helix

391 – 393

3

Helix

394 – 413

20

Sequences

	Sequence		Length	Mass (Da)
	P15086 [UniParc]. Last modified May 10, 2002. Version 4. Checksum: EBBB98B27F5D5AF9	FASTA	417	47,368
	10 20 30 40 50 60 MLALLVLVTV ALASAHHGGE HFEGEKVFRV NVEDENHINI IRELASTTQI DFWKPDSVTQ 70 80 90 100 110 120 IKPHSTVDFR VKAEDTVTVE NVLKQNELQY KVLISNLRNV VEAQFDSRVR ATGHSYEKYN 130 140 150 160 170 180 KWETIEAWTQ QVATENPALI SRSVIGTTFE GRAIYLLKVG KAGQNKPAIF MDCGFHAREW 190 200 210 220 230 240 ISPAFCQWFV REAVRTYGRE IQVTELLDKL DFYVLPVLNI DGYIYTWTKS RFWRKTRSTH 250 260 270 280 290 300 TGSSCIGTDP NRNFDAGWCE IGASRNPCDE TYCGPAAESE KETKALADFI RNKLSSIKAY 310 320 330 340 350 360 LTIHSYSQMM IYPYSYAYKL GENNAELNAL AKATVKELAS LHGTKYTYGP GATTIYPAAG 370 380 390 400 410 GSDDWAYDQG IRYSFTFELR DTGRYGFLLP ESQIRATCEE TFLAIKYVAS YVLEHLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a cDNA encoding a human serum marker for acute pancreatitis. Identification of pancreas-specific protein as pancreatic procarboxypeptidase B." Yamamoto K.K., Pousette A., Chow P., Wilson H., el Shami S., French C.K. J. Biol. Chem. 267:2575-2581(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-40. Tissue: Pancreas.
[2]	"Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B." Aloy P., Catasus L., Villegas V., Reverter D., Vendrell J., Aviles F.X. Biol. Chem. 379:149-155(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-208. Tissue: Pancreas.
[3]	"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Adrenal gland.
[6]	"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 16-43. Tissue: Pancreas.
[7]	"Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)." Barbosa-Pereira P.J., Segura-Martin S., Oliva B., Ferrer-Orta C., Aviles F.X., Coll M., Gomis-Ruth F.X., Vendrell J. J. Mol. Biol. 321:537-547(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 16-417.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M81057 mRNA. Translation: AAA66973.1.
AJ224866 mRNA. Translation: CAA12163.1.
BT009910 mRNA. Translation: AAP88912.1.
CH471052 Genomic DNA. Translation: EAW78903.1.
BC015338 mRNA. Translation: AAH15338.1.

IPI

IPI00009826.

PIR

A42332.

RefSeq

NP_001862.2. NM_001871.2.

UniGene

Hs.477891.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KWM	X-ray	1.60	A/B	16-417	[»]
1ZLI	X-ray	2.09	A	109-417	[»]

ProteinModelPortal

P15086.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000282957.

Protein family/group databases

MEROPS

M14.003.

Polymorphism databases

DMDM

20532382.

Proteomic databases

PaxDb

P15086.

PRIDE

P15086.

Protocols and materials databases

DNASU

1360.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000282957; ENSP00000282957; ENSG00000153002.
ENST00000491148; ENSP00000417222; ENSG00000153002.

GeneID

1360.

KEGG

hsa:1360.

UCSC

uc003ewl.3. human.

Organism-specific databases

CTD

1360.

GeneCards

GC03P148508.

HGNC

HGNC:2299. CPB1.

MIM

114852. gene.

neXtProt

NX_P15086.

PharmGKB

PA26821.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2866.

HOGENOM

HOG000252968.

HOVERGEN

HBG050815.

InParanoid

P15086.

KO

K01291.

OMA

WKPDSAT.

OrthoDB

EOG4PVNZR.

PhylomeDB

P15086.

Gene expression databases

ArrayExpress

P15086.

Bgee

P15086.

CleanEx

HS_CPB1.

Genevestigator

P15086.

GermOnline

ENSG00000153002. 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

P15086.

ChEMBL

CHEMBL2552.

ChiTaRS

CPB1. human.

EvolutionaryTrace

P15086.

GenomeRNAi

1360.

NextBio

5509.

PMAP-CutDB

P15086.

SOURCE

Search...

Entry information

Entry name

CBPB1_HUMAN

Accession

Primary (citable) accession number: P15086
Secondary accession number(s): O60834, Q53XJ0, Q96BQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 10, 2002
Last modified:	May 1, 2013
This is version 147 of the entry and version 4 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.