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Protein

Atrial natriuretic peptide-converting enzyme

Gene

Corin

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei908 – 9081Charge relay systemPROSITE-ProRule annotation
Active sitei957 – 9571Charge relay systemPROSITE-ProRule annotation
Active sitei1050 – 10501Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  • scavenger receptor activity Source: InterPro
  • serine-type endopeptidase activity Source: RGD

GO - Biological processi

  • female pregnancy Source: UniProtKB
  • peptide hormone processing Source: UniProtKB
  • protein processing Source: RGD
  • proteolysis Source: RGD
  • regulation of blood pressure Source: UniProtKB
  • regulation of renal sodium excretion Source: UniProtKB
  • regulation of systemic arterial blood pressure by atrial natriuretic peptide Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.019.

Names & Taxonomyi

Protein namesi
Recommended name:
Atrial natriuretic peptide-converting enzyme (EC:3.4.21.-)
Alternative name(s):
Corin
Pro-ANP-converting enzyme
Cleaved into the following 3 chains:
Gene namesi
Name:Corin
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi727887. Corin.

Subcellular locationi

Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment :
  • Secreted By similarity

  • Note: Soluble form produced following cleavage by ADAM10.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 112112CytoplasmicSequence analysisAdd
BLAST
Transmembranei113 – 13321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini134 – 1111978ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi866 – 8661R → A: Impairs proteolytic processing and activation. 1 Publication
Mutagenesisi968 – 9681N → S: Prevents proteolytic processing and activation; when associated with S-1087. 1 Publication
Mutagenesisi1087 – 10871N → S: Prevents proteolytic processing and activation; when associated with S-968. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 866Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragmentBy similarityPRO_0000417988
Chaini1 – 11111111Atrial natriuretic peptide-converting enzymePRO_0000391762Add
BLAST
Chaini1 – 866866Atrial natriuretic peptide-converting enzyme, N-terminal propeptideCuratedPRO_0000391763Add
BLAST
Chaini867 – 1111245Atrial natriuretic peptide-converting enzyme, activated protease fragmentCuratedPRO_0000391764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence analysis
Disulfide bondi204 ↔ 264By similarity
Disulfide bondi212 ↔ 257By similarity
Disulfide bondi248 ↔ 288By similarity
Disulfide bondi277 ↔ 322By similarity
Disulfide bondi281 ↔ 305By similarity
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence analysis
Disulfide bondi335 ↔ 348By similarity
Disulfide bondi343 ↔ 361By similarity
Disulfide bondi355 ↔ 370By similarity
Disulfide bondi372 ↔ 384By similarity
Disulfide bondi379 ↔ 397By similarity
Disulfide bondi391 ↔ 406By similarity
Disulfide bondi408 ↔ 421By similarity
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi416 ↔ 434By similarity
Disulfide bondi428 ↔ 443By similarity
Disulfide bondi445 ↔ 458By similarity
Disulfide bondi453 ↔ 471By similarity
Disulfide bondi465 ↔ 480By similarity
Disulfide bondi521 ↔ 584By similarity
Disulfide bondi529 ↔ 577By similarity
Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi568 ↔ 606By similarity
Disulfide bondi595 ↔ 636By similarity
Disulfide bondi599 ↔ 623By similarity
Disulfide bondi646 ↔ 658By similarity
Disulfide bondi653 ↔ 671By similarity
Disulfide bondi665 ↔ 680By similarity
Disulfide bondi682 ↔ 696By similarity
Disulfide bondi690 ↔ 709By similarity
Disulfide bondi703 ↔ 718By similarity
Disulfide bondi721 ↔ 733By similarity
Disulfide bondi728 ↔ 746By similarity
Disulfide bondi740 ↔ 755By similarity
Glycosylationi763 – 7631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi855 ↔ 977Interchain (between N-terminal propeptide and activated protease fragment chains)PROSITE-ProRule annotation
Disulfide bondi893 ↔ 909By similarity
Disulfide bondi991 ↔ 1056By similarity
Disulfide bondi1020 ↔ 1035By similarity

Post-translational modificationi

N-glycosylated; required for processing and activation.1 Publication
Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1 (Probable).1 Publication
A disulfide bond links the activated corin protease fragment and the N-terminal propeptide. The disulfide bond also links the activated corin protease fragment with Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment (Probable).Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei866 – 8672CleavageCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ80YN4.

Expressioni

Tissue specificityi

Specifically expressed in heart. Also detected in kidney, aorta, brain and testis. In kidney, present in epithelial cells, with segmental expression in the proximal tubule, thick ascending limb, connecting tubule, and throughout the collecting duct (at protein level).1 Publication

Inductioni

Down-regulated upon experimental heart failure.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 325127FZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini334 – 37138LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini371 – 40737LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini407 – 44438LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini444 – 48138LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini516 – 639124FZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini645 – 68137LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini681 – 71939LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini720 – 75637LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini756 – 85196SRCRPROSITE-ProRule annotationAdd
BLAST
Domaini867 – 1100234Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi93 – 964DDNN motif

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 FZ (frizzled) domains.PROSITE-ProRule annotation
Contains 7 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SRCR domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000060148.
HOVERGENiHBG051079.
InParanoidiQ80YN4.
KOiK09614.

Family and domain databases

Gene3Di1.10.2000.10. 2 hits.
3.10.250.10. 1 hit.
4.10.400.10. 6 hits.
InterProiIPR017052. Corin.
IPR020067. Frizzled_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF01392. Fz. 2 hits.
PF00057. Ldl_recept_a. 6 hits.
PF15494. SRCR_2. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF036376. Corin. 1 hit.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00063. FRI. 2 hits.
SM00192. LDLa. 7 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 7 hits.
SSF63501. SSF63501. 2 hits.
PROSITEiPS50038. FZ. 2 hits.
PS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 7 hits.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80YN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRVSFNVRV SSVRRARCSC PGRCYLSCRV PPTTALHALN GFGRAGVLGE
60 70 80 90 100
TAGGTVGLGP SGTRGFLSGS KFQASGSLKD CFGAPPAPDV LRADSSVGEG
110 120 130 140 150
CPQKLVTANL LRFLLLVLIP CICALIVLLA ILLSFVGTLK KVYFKSNDSE
160 170 180 190 200
PLVTDGEVRV PGVIHVNRYE NTGAPSMPPS QSIPAWTPRA PSLEDQSHGN
210 220 230 240 250
TSTCVNITHR QCQILPYHST LAPLLPIVKN MDTEKFLKFF TYLHRLGCYQ
260 270 280 290 300
HILLFGCSLA FPKCIVDGDD RHGLLPCRSF CEAAKEGCES VLGMVNSSWP
310 320 330 340 350
DSLRCSQFRY HTENNSDASR ICFSLQQEHG KQSLCGGGES FLCTSGLCIS
360 370 380 390 400
KKLQCNGYND CDDWSDEAHC NCSEDLFHCG TGKCLHHSLV CDGYDDCGDL
410 420 430 440 450
SDEQNCDCNL TKEHRCGDGR CIAAEWVCDG DHDCVDKSDE VNCSCPSQGL
460 470 480 490 500
VECRSGQCIP STFQCDGDED CKDGSDEENC SDRPTPCPGG DRGCLDSSCV
510 520 530 540 550
ESCAGSSLCD SDSSLSNCSH CEPITLELCM NLPYNLTHYP NYLGHRTQKE
560 570 580 590 600
ASISWESALF PALVQTNCYK YLMFFACTIL VPKCDVNTGQ RVPPCRLLCE
610 620 630 640 650
HSKERCESVL GIVGLQWPED TDCSQFPEQS SDNQTCLLPN EDVEECSPSH
660 670 680 690 700
FKCRSGRCVL GSRRCDGQAD CDDDSDEENC GCKERDLWEC PLNKQCLKHT
710 720 730 740 750
LICDGFPDCS DSMDEKNCSF CQDDELECAN HECVPRDLWC DGWTDCSDSS
760 770 780 790 800
DEWGCVTLSK NGNSSSFLTV HRSARDHHVC ADGWQETLSQ LACRQMGLGE
810 820 830 840 850
PSVTELVQGQ EGQQWLRLHS SWENLNGSTL QELLVHRRSC PSGSEISLLC
860 870 880 890 900
TKQDCGRRPA ARMNKRILGG RTSRPGRWPW QCSLQSEPSG HICGCVLIAK
910 920 930 940 950
KWVLTVAHCF EGREDADVWK VVFGINNLDH PSGFMQTRFV KTILLHPRYS
960 970 980 990 1000
RAVVDYDISV VELSDDINET SYVRPVCLPS PREFLEPDTY CYITGWGHMG
1010 1020 1030 1040 1050
NKMPFKLQEG EVRIIPLEQC QSYFDMKTIT NRMICAGYES GTVDSCMIDS
1060 1070 1080 1090 1100
GGPLVCERPG GQWTLFGLTS WGSVCFSKVL GPGVYSNVSY FVDWIERQIY
1110
IQTFLQKKSQ G
Length:1,111
Mass (Da):122,757
Last modified:June 13, 2012 - v2
Checksum:i44A738ACA6E0AC16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781P → S in AAO86772 (PubMed:15155264).Curated
Sequence conflicti320 – 3201R → T in AAO86772 (PubMed:15155264).Curated
Sequence conflicti1048 – 10481I → G in AAO86772 (PubMed:15155264).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY251285 mRNA. Translation: AAO86772.1.
AC121481 Genomic DNA. No translation available.
RefSeqiNP_872279.1. NM_182473.1.
UniGeneiRn.211679.

Genome annotation databases

GeneIDi289596.
KEGGirno:289596.
UCSCiRGD:727887. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY251285 mRNA. Translation: AAO86772.1.
AC121481 Genomic DNA. No translation available.
RefSeqiNP_872279.1. NM_182473.1.
UniGeneiRn.211679.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061602.

Protein family/group databases

MEROPSiS01.019.

Proteomic databases

PaxDbiQ80YN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi289596.
KEGGirno:289596.
UCSCiRGD:727887. rat.

Organism-specific databases

CTDi10699.
RGDi727887. Corin.

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000060148.
HOVERGENiHBG051079.
InParanoidiQ80YN4.
KOiK09614.

Miscellaneous databases

PROiQ80YN4.

Family and domain databases

Gene3Di1.10.2000.10. 2 hits.
3.10.250.10. 1 hit.
4.10.400.10. 6 hits.
InterProiIPR017052. Corin.
IPR020067. Frizzled_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF01392. Fz. 2 hits.
PF00057. Ldl_recept_a. 6 hits.
PF15494. SRCR_2. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF036376. Corin. 1 hit.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00063. FRI. 2 hits.
SM00192. LDLa. 7 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 7 hits.
SSF63501. SSF63501. 2 hits.
PROSITEiPS50038. FZ. 2 hits.
PS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 7 hits.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat corin gene: molecular cloning and reduced expression in experimental heart failure."
    Langenickel T.H., Pagel I., Buttgereit J., Tenner K., Lindner M., Dietz R., Willenbrock R., Bader M.
    Am. J. Physiol. 287:H1516-H1521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: Sprague-Dawley.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Role of glycosylation in corin zymogen activation."
    Liao X., Wang W., Chen S., Wu Q.
    J. Biol. Chem. 282:27728-27735(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIVATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-866; ASN-968 AND ASN-1087, GLYCOSYLATION, SUBCELLULAR LOCATION.
  4. "Decreased renal corin expression contributes to sodium retention in proteinuric kidney diseases."
    Polzin D., Kaminski H.J., Kastner C., Wang W., Kramer S., Gambaryan S., Russwurm M., Peters H., Wu Q., Vandewalle A., Bachmann S., Theilig F.
    Kidney Int. 78:650-659(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCORIN_RAT
AccessioniPrimary (citable) accession number: Q80YN4
Secondary accession number(s): D3ZN44, F1LS60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 13, 2012
Last modified: June 8, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.