FUNCTION: Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin (By similarity).
CATALYTIC ACTIVITY: Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Periplasm (By similarity).
SIMILARITY: Belongs to the peptidase M16 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE014075; AAN81860.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_755290.1; -.

3D structure databases

SMR

Q8CVS2; 24-960.

ModBase

Q8CVS2.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR011237; Pept_M16_core.
IPR011765; Pept_M16_N.
IPR001431; Pept_M16_Zn_BS.
IPR007863; Peptidase_M16_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.830.10; Pept_M16_core; 1.

Pfam

PF00675; Peptidase_M16; 1.
PF05193; Peptidase_M16_C; 2.
Pfam graphical view of domain structure.

PROSITE

PS00143; INSULINASE; 1.

Genome annotation databases

GeneID

1039287; -.

GenomeReviews

AE014075_GR; c3415.

KEGG

ecc:c3415; -.

Phylogenomic databases

HOGENOM

Q8CVS2; -.

Genome annotation databases

CMR

Q8CVS2; c3415.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; Magnesium; Metal-binding; Metalloprotease; Periplasm; Protease; Signal; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`By similarity.`
`CHAIN`	`24 962`	`939`	`Protease 3.`	`PRO_0000026760`
`ACT_SITE`	`91 91`		`Proton acceptor (By similarity).`
`METAL`	`88 88`		`Zinc (By similarity).`
`METAL`	`92 92`		`Zinc (By similarity).`
`METAL`	`169 169`		`Zinc (By similarity).`

Sequence information

Length: 962 AA [This is the length of the unprocessed precursor]

Molecular weight: 107892 Da [This is the MW of the unprocessed precursor]

CRC64: DEDD2CA2A9AADF8D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPRSIWFKAL LLFVALWAPL SQAETGWQPI QETIRKSDKD NRQYQAIRLD NGMVVLLVSD 

        70         80         90        100        110        120 
PQAVKSLSAL VVPVGSLEDP EAYQGLAHYL EHMSLMGSKK YPQADSLAEY LKMHGGSHNA 

       130        140        150        160        170        180 
STAPYRTAFY LEVENDALPG AVDRLADAIA EPLLDKKYAE RERNAVNAEL TMARTRDGMR 

       190        200        210        220        230        240 
MAQVSAETIN PAHPGSKFSG GNLETLSDKP GNPVQQALKD FHEKYYSANL MKAVIYSNKP 

       250        260        270        280        290        300 
LPELAKMAAD TFGRVPNKES KKPEITVPVV TDAQKGIIIH YVPALPRKVL RVEFRIDNNS 

       310        320        330        340        350        360 
AKFRSKTDEL ITYLIGNRSP GTLSDWLQKQ GLVEGISANS DPIVNGNSGV LAISASLTDK 

       370        380        390        400        410        420 
GLANRDQVVA AIFSYLNLLR EKGIDKQYFD ELANVLDIDF RYPSITRDMD YVEWLADTMI 

       430        440        450        460        470        480 
RVPVEHTLDA VNIADRYDAK AVKERLAMMT PQNARIWYIS PKEPHNKTAY FVDAPYQVDK 

       490        500        510        520        530        540 
ISEQTFADWQ KKAANIALSL PELNPYIPDD FSLIKSEKKY DHPELIVDES NLRVVYAPSR 

       550        560        570        580        590        600 
YFASEPKADV SLILRNPKAM DSARNQVMFA LNDYLAGLAL DQLSNQASVG GISFSTNANN 

       610        620        630        640        650        660 
GLMVNANGYT QRLPQLFQAL LEGYFSYTAT EDQLEQAKSW YNQMMDSAEK GKAFEQAIMP 

       670        680        690        700        710        720 
AQMLSQVPYF SRDERRKILP SITLKEVLAY RDALKSGARP EFMVIGNMTE AQATTLARHV 

       730        740        750        760        770        780 
QKQLGADGSE WCRNKDVVVD KKQSVIFEKA GNSTDSALAA IFVPTGYDEY TSSAYSSLLG 

       790        800        810        820        830        840 
QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS NDKQPSFLWE RYKAFFPTAE 

       850        860        870        880        890        900 
AKLRTMKPEE FAQIQQAVIT QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL 

       910        920        930        940        950        960 
TPQKLADFFH QAVVEPQGMA ILSQISGSQN GKAEYVHPEG WKVWENVSAL QQTMPLMSEK 


NE

Q8CVS2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools