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Q80W65 (PCSK9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proprotein convertase subtilisin/kexin type 9

EC=3.4.21.-
Alternative name(s):
Neural apoptosis-regulated convertase 1
Short name=NARC-1
Proprotein convertase 9
Short name=PC9
Subtilisin/kexin-like protease PC9
Gene names
Name:Pcsk9
Synonyms:Narc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na+ channel (ENaC)-mediated Na+ absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways. Ref.9 Ref.10

Cofactor

Calcium Probable.

Enzyme regulation

Its proteolytic activity is autoinhibited by the non-covalent binding of the propeptide to the catalytic domain. Inhibited by EGTA.

Subunit structure

Monomer. Can self-associate to form dimers and higher multimers which may have increased LDLR degrading activity. The precursor protein but not the mature protein may form multimers. Interacts with APOB, VLDLR, LRP8/APOER2 and BACE1. The full length immature form (pro-PCSK9) interacts with SCNN1A, SCNN1B and SCNN1G. The pro-PCSK9 form (via C-terminal domain) interacts with LDLR By similarity.

Subcellular location

Cytoplasm By similarity. Secreted. Endosome By similarity. Lysosome By similarity. Cell surface By similarity. Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Note: Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and co-localizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation By similarity.

Tissue specificity

Hepatocytes, kidney mesenchymal cells, intestinal ileum, colon epithelia and embryonic brain telencephalon neurons.

Developmental stage

In the embryo, expressed in the liver at day E9, in the skin and transiently in the telencephalon at day E12, and in the kidney, small intestine and cerebellum at E15.

Induction

Down-regulated following a high-cholesterol diet. Ref.2

Domain

The C-terminal domain (CRD) is essential for the LDLR-binding and degrading activities By similarity.

The catalytic domain is responsible for mediating its self-association By similarity.

Post-translational modification

Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation By similarity.

Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein By similarity. Ref.6 Ref.7

Phosphorylation protects the propeptide against proteolysis By similarity.

Sequence similarities

Belongs to the peptidase S8 family.

Contains 1 peptidase S8 domain.

Sequence caution

The sequence AAP31672.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE28934.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAC60362.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Cholesterol metabolism
Lipid metabolism
Steroid metabolism
Sterol metabolism
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Secreted
   DomainSignal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Phosphoprotein
Sulfation
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to insulin stimulus

Inferred from direct assay PubMed 16407292. Source: HGNC

cellular response to starvation

Inferred from direct assay PubMed 16407292. Source: HGNC

cholesterol homeostasis

Inferred from sequence or structural similarity Ref.6. Source: HGNC

cholesterol metabolic process

Inferred from direct assay PubMed 17242417. Source: MGI

kidney development

Inferred from expression pattern Ref.6. Source: HGNC

lipoprotein metabolic process

Inferred from direct assay PubMed 17242417. Source: MGI

liver development

Inferred from expression pattern Ref.6. Source: HGNC

low-density lipoprotein particle receptor catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

low-density lipoprotein receptor particle metabolic process

Inferred from direct assay PubMed 17242417. Source: MGI

lysosomal transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of catalytic activity

Inferred from electronic annotation. Source: InterPro

negative regulation of low-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Ensembl

negative regulation of receptor recycling

Inferred from electronic annotation. Source: Ensembl

neurogenesis

Inferred from expression pattern Ref.6. Source: HGNC

neuron differentiation

Inferred from direct assay PubMed 16893422. Source: HGNC

phospholipid metabolic process

Inferred from direct assay PubMed 17242417. Source: MGI

positive regulation of neuron apoptotic process

Inferred from sequence or structural similarity Ref.6. Source: HGNC

positive regulation of receptor internalization

Inferred from electronic annotation. Source: Ensembl

protein autoprocessing

Inferred from sequence or structural similarity Ref.6. Source: HGNC

proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of low-density lipoprotein particle receptor catabolic process

Inferred from mutant phenotype PubMed 15741654PubMed 15805190. Source: MGI

regulation of neuron apoptotic process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from direct assay PubMed 17242417. Source: MGI

   Cellular_componentER to Golgi transport vesicle

Inferred from direct assay PubMed 23580231. Source: MGI

Golgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Inferred from direct assay Ref.6. Source: MGI

extracellular space

Inferred from direct assay PubMed 17080197. Source: HGNC

late endosome

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionapolipoprotein binding

Inferred from direct assay Ref.9. Source: UniProtKB

low-density lipoprotein particle binding

Inferred from direct assay Ref.9. Source: UniProtKB

low-density lipoprotein particle receptor binding

Inferred from direct assay PubMed 17080197. Source: HGNC

protein self-association

Inferred from sequence or structural similarity. Source: UniProtKB

serine-type endopeptidase activity

Inferred from sequence or structural similarity Ref.6. Source: HGNC

sodium channel inhibitor activity

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Propeptide35 – 155121
PRO_0000027122
Chain156 – 694539Proprotein convertase subtilisin/kexin type 9
PRO_0000027123

Regions

Domain166 – 432267Peptidase S8
Region156 – 452297Catalytic domain By similarity
Region453 – 694242C-terminal domain By similarity
Motif499 – 5013Cell attachment site Potential

Sites

Active site1891Charge relay system By similarity
Active site2291Charge relay system By similarity
Active site3891Charge relay system By similarity
Site155 – 1562Cleavage; by autolysis By similarity
Site221 – 2222Cleavage; by furin and PCSK5 By similarity

Amino acid modifications

Modified residue411Sulfotyrosine By similarity
Modified residue501Phosphoserine Ref.8
Modified residue6911Phosphoserine By similarity
Glycosylation5361N-linked (GlcNAc...) By similarity
Disulfide bond226 ↔ 258 Potential
Disulfide bond326 ↔ 361 Potential
Disulfide bond460 ↔ 530 Potential
Disulfide bond480 ↔ 529 Potential
Disulfide bond489 ↔ 512 Potential
Disulfide bond537 ↔ 604 Potential
Disulfide bond555 ↔ 603 Potential
Disulfide bond565 ↔ 591 Potential
Disulfide bond611 ↔ 682 Potential
Disulfide bond629 ↔ 681 Potential
Disulfide bond638 ↔ 657 Potential

Experimental info

Sequence conflict17 – 193Missing in CAC60362. Ref.1
Sequence conflict341A → T in CAC60362. Ref.1
Sequence conflict1891D → G in CAC60362. Ref.1
Sequence conflict1961H → Y in CAC60362. Ref.1
Sequence conflict2001E → A in CAC60362. Ref.1
Sequence conflict3051R → Q in CAC60362. Ref.1
Sequence conflict5341R → H in CAC60362. Ref.1
Sequence conflict6261T → A in CAC60362. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80W65 [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: 977BD4BD1FAF98C0

FASTA69474,823
        10         20         30         40         50         60 
MGTHCSAWLR WPLLPLLPPL LLLLLLLCPT GAGAQDEDGD YEELMLALPS QEDGLADEAA 

        70         80         90        100        110        120 
HVATATFRRC SKEAWRLPGT YIVVLMEETQ RLQIEQTAHR LQTRAARRGY VIKVLHIFYD 

       130        140        150        160        170        180 
LFPGFLVKMS SDLLGLALKL PHVEYIEEDS FVFAQSIPWN LERIIPAWHQ TEEDRSPDGS 

       190        200        210        220        230        240 
SQVEVYLLDT SIQGAHREIE GRVTITDFNS VPEEDGTRFH RQASKCDSHG THLAGVVSGR 

       250        260        270        280        290        300 
DAGVAKGTSL HSLRVLNCQG KGTVSGTLIG LEFIRKSQLI QPSGPLVVLL PLAGGYSRIL 

       310        320        330        340        350        360 
NAACRHLART GVVLVAAAGN FRDDACLYSP ASAPEVITVG ATNAQDQPVT LGTLGTNFGR 

       370        380        390        400        410        420 
CVDLFAPGKD IIGASSDCST CFMSQSGTSQ AAAHVAGIVA RMLSREPTLT LAELRQRLIH 

       430        440        450        460        470        480 
FSTKDVINMA WFPEDQQVLT PNLVATLPPS THETGGQLLC RTVWSAHSGP TRTATATARC 

       490        500        510        520        530        540 
APEEELLSCS SFSRSGRRRG DWIEAIGGQQ VCKALNAFGG EGVYAVARCC LVPRANCSIH 

       550        560        570        580        590        600 
NTPAARAGLE THVHCHQKDH VLTGCSFHWE VEDLSVRRQP ALRSRRQPGQ CVGHQAASVY 

       610        620        630        640        650        660 
ASCCHAPGLE CKIKEHGISG PSEQVTVACE AGWTLTGCNV LPGASLTLGA YSVDNLCVAR 

       670        680        690 
VHDTARADRT SGEATVAAAI CCRSRPSAKA SWVQ 

« Hide

References

« Hide 'large scale' references
[1]"Narc-1, novel subtilase-like homologs."
Chiang L.W.
Patent number WO0157081, 09-AUG-2001
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Novel putative SREBP and LXR target genes identified by microarray analysis in liver of cholesterol-fed mice."
Maxwell K.N., Soccio R.E., Duncan E.M., Sehayek E., Breslow J.L.
J. Lipid Res. 44:2109-2119(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: C57BL/6.
Tissue: Liver.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Strain: C57BL/6.
Tissue: Eye.
[6]"The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation."
Seidah N.G., Benjannet S., Wickham L., Marcinkiewicz J., Jasmin S.B., Stifani S., Basak A., Prat A., Chretien M.
Proc. Natl. Acad. Sci. U.S.A. 100:928-933(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROPEPTIDE CLEAVAGE SITE, CHARACTERIZATION.
[7]"Functional characterization of Narc 1, a novel proteinase related to proteinase K."
Naureckiene S., Ma L., Sreekumar K., Purandare U., Lo C.F., Huang Y., Chiang L.W., Grenier J.M., Ozenberger B.A., Jacobsen J.S., Kennedy J.D., DiStefano P.S., Wood A., Bingham B.
Arch. Biochem. Biophys. 420:55-67(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOCATALYTIC CLEAVAGE SITE.
[8]"PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans."
Dewpura T., Raymond A., Hamelin J., Seidah N.G., Mbikay M., Chretien M., Mayne J.
FEBS J. 275:3480-3493(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Proprotein convertase subtilisin/kexin type 9 interacts with apolipoprotein B and prevents its intracellular degradation, irrespective of the low-density lipoprotein receptor."
Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.
Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"PCSK9 regulates neuronal apoptosis by adjusting ApoER2 levels and signaling."
Kysenius K., Muggalla P., Maetlik K., Arumaee U., Huttunen H.J.
Cell. Mol. Life Sci. 69:1903-1916(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AX207688 Unassigned DNA. Translation: CAC60362.1. Different initiation.
AY273821 mRNA. Translation: AAP31672.1. Different initiation.
AK149520 mRNA. Translation: BAE28934.1. Different initiation.
AL954352 Genomic DNA. Translation: CAM15751.1.
BC038085 mRNA. Translation: AAH38085.1.
RefSeqNP_705793.1. NM_153565.2.
UniGeneMm.133268.

3D structure databases

ProteinModelPortalQ80W65.
SMRQ80W65. Positions 64-685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000055757.

Protein family/group databases

MEROPSS08.039.

PTM databases

PhosphoSiteQ80W65.

Proteomic databases

PaxDbQ80W65.
PRIDEQ80W65.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049507; ENSMUSP00000055757; ENSMUSG00000044254.
GeneID100102.
KEGGmmu:100102.
UCSCuc008tyi.2. mouse.

Organism-specific databases

CTD255738.
MGIMGI:2140260. Pcsk9.

Phylogenomic databases

eggNOGCOG1404.
GeneTreeENSGT00490000043472.
HOGENOMHOG000049267.
HOVERGENHBG053530.
InParanoidB1AZI4.
KOK13050.
OMACHAPGLE.
OrthoDBEOG79PJNT.
PhylomeDBQ80W65.
TreeFamTF106271.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

BgeeQ80W65.
CleanExMM_PCSK9.
GenevestigatorQ80W65.

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR010259. Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
[Graphical view]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
ProtoNetSearch...

Other

NextBio354261.
PROQ80W65.
SOURCESearch...

Entry information

Entry namePCSK9_MOUSE
AccessionPrimary (citable) accession number: Q80W65
Secondary accession number(s): B1AZI4 expand/collapse secondary AC list , Q3UEH7, Q8BXW9, Q8CFT6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: April 16, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot