Proprotein convertase subtilisin/kexin type 5

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• endopeptidase activity Source: ReactomeInferred from experimentⁱ
  • "Proprotein convertases are responsible for proteolysis and inactivation of endothelial lipase."
    Jin W., Fuki I.V., Seidah N.G., Benjannet S., Glick J.M., Rader D.J.
    J Biol Chem 280:36551-36559(2005) [PubMed] [Europe PMC] [Abstract]
  • "Angiopoietin-like protein 3 inhibits lipoprotein lipase activity through enhancing its cleavage by proprotein convertases."
    Liu J., Afroza H., Rader D.J., Jin W.
    J. Biol. Chem. 285:27561-27570(2010) [PubMed] [Europe PMC] [Abstract]
• peptidase activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Beta-amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furin."
    Wickham L., Benjannet S., Marcinkiewicz E., Chretien M., Seidah N.G.
    J. Neurochem. 92:93-102(2005) [PubMed] [Europe PMC] [Abstract]
• peptide binding Source: BHF-UCL <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]
• serine-type endopeptidase activity Source: BHF-UCLInferred from direct assayⁱ
  • "Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex."
    Mercure C., Jutras I., Day R., Seidah N.G., Reudelhuber T.L.
    Hypertension 28:840-846(1996) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• anterior/posterior pattern specification Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "VACTERL/caudal regression/Currarino syndrome-like malformations in mice with mutation in the proprotein convertase Pcsk5."
    Szumska D., Pieles G., Essalmani R., Bilski M., Mesnard D., Kaur K., Franklyn A., El Omari K., Jefferis J., Bentham J., Taylor J.M., Schneider J.E., Arnold S.J., Johnson P., Tymowska-Lalanne Z., Stammers D., Clarke K., Neubauer S.

    , Morris A., Brown S.D., Shaw-Smith C., Cama A., Capra V., Ragoussis J., Constam D., Seidah N.G., Prat A., Bhattacharya S.
    Genes Dev 22:1465-1477(2008) [PubMed] [Europe PMC] [Abstract]
• cell-cell signaling Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex."
    Mercure C., Jutras I., Day R., Seidah N.G., Reudelhuber T.L.
    Hypertension 28:840-846(1996) [PubMed] [Europe PMC] [Abstract]
• cytokine precursor processing Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]
• embryo implantation Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]
• embryonic digestive tract development Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "VACTERL/caudal regression/Currarino syndrome-like malformations in mice with mutation in the proprotein convertase Pcsk5."
    Szumska D., Pieles G., Essalmani R., Bilski M., Mesnard D., Kaur K., Franklyn A., El Omari K., Jefferis J., Bentham J., Taylor J.M., Schneider J.E., Arnold S.J., Johnson P., Tymowska-Lalanne Z., Stammers D., Clarke K., Neubauer S.

    , Morris A., Brown S.D., Shaw-Smith C., Cama A., Capra V., Ragoussis J., Constam D., Seidah N.G., Prat A., Bhattacharya S.
    Genes Dev 22:1465-1477(2008) [PubMed] [Europe PMC] [Abstract]
• embryonic skeletal system development Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "VACTERL/caudal regression/Currarino syndrome-like malformations in mice with mutation in the proprotein convertase Pcsk5."
    Szumska D., Pieles G., Essalmani R., Bilski M., Mesnard D., Kaur K., Franklyn A., El Omari K., Jefferis J., Bentham J., Taylor J.M., Schneider J.E., Arnold S.J., Johnson P., Tymowska-Lalanne Z., Stammers D., Clarke K., Neubauer S.

    , Morris A., Brown S.D., Shaw-Smith C., Cama A., Capra V., Ragoussis J., Constam D., Seidah N.G., Prat A., Bhattacharya S.
    Genes Dev 22:1465-1477(2008) [PubMed] [Europe PMC] [Abstract]
• heart development Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]
• kidney development Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "VACTERL/caudal regression/Currarino syndrome-like malformations in mice with mutation in the proprotein convertase Pcsk5."
    Szumska D., Pieles G., Essalmani R., Bilski M., Mesnard D., Kaur K., Franklyn A., El Omari K., Jefferis J., Bentham J., Taylor J.M., Schneider J.E., Arnold S.J., Johnson P., Tymowska-Lalanne Z., Stammers D., Clarke K., Neubauer S.

    , Morris A., Brown S.D., Shaw-Smith C., Cama A., Capra V., Ragoussis J., Constam D., Seidah N.G., Prat A., Bhattacharya S.
    Genes Dev 22:1465-1477(2008) [PubMed] [Europe PMC] [Abstract]
• limb morphogenesis Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]
• nerve growth factor processing Source: Reactome
• peptide biosynthetic process Source: BHF-UCLInferred from direct assayⁱ
  • "Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex."
    Mercure C., Jutras I., Day R., Seidah N.G., Reudelhuber T.L.
    Hypertension 28:840-846(1996) [PubMed] [Europe PMC] [Abstract]
• peptide hormone processing Source: BHF-UCLInferred from direct assayⁱ
  • "Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex."
    Mercure C., Jutras I., Day R., Seidah N.G., Reudelhuber T.L.
    Hypertension 28:840-846(1996) [PubMed] [Europe PMC] [Abstract]
• protein processing Source: BHF-UCLInferred from direct assayⁱ
  • "Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex."
    Mercure C., Jutras I., Day R., Seidah N.G., Reudelhuber T.L.
    Hypertension 28:840-846(1996) [PubMed] [Europe PMC] [Abstract]
• regulation of lipoprotein lipase activity Source: Reactome
• renin secretion into blood stream Source: BHF-UCL <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex."
    Mercure C., Jutras I., Day R., Seidah N.G., Reudelhuber T.L.
    Hypertension 28:840-846(1996) [PubMed] [Europe PMC] [Abstract]
• respiratory tube development Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]
• signal peptide processing Source: HGNC-UCLInferred from direct assayⁱ
  • "The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications."
    Benjannet S., Rhainds D., Hamelin J., Nassoury N., Seidah N.G.
    J. Biol. Chem. 281:30561-30572(2006) [PubMed] [Europe PMC] [Abstract]
• viral life cycle Source: BHF-UCLInferred from expression patternⁱ
  • "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines."
    Decroly E., Wouters S., Di Bello C., Lazure C., Ruysschaert J.M., Seidah N.G.
    J Biol Chem 271:30442-30450(1996) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Sites

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Motif

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MGWGSRCCCP GRLDLLCVLA LLGGCLLPVC RTRVYTNHWA VKIAGGFPEA 
        60         70         80         90        100
NRIASKYGFI NIGQIGALKD YYHFYHSRTI KRSVISSRGT HSFISMEPKV 
       110        120        130        140        150
EWIQQQVVKK RTKRDYDFSR AQSTYFNDPK WPSMWYMHCS DNTHPCQSDM 
       160        170        180        190        200
NIEGAWKRGY TGKNIVVTIL DDGIERTHPD LMQNYDALAS CDVNGNDLDP 
       210        220        230        240        250
MPRYDASNEN KHGTRCAGEV AAAANNSHCT VGIAFNAKIG GVRMLDGDVT 
       260        270        280        290        300
DMVEAKSVSF NPQHVHIYSA SWGPDDDGKT VDGPAPLTRQ AFENGVRMGR 
       310        320        330        340        350
RGLGSVFVWA SGNGGRSKDH CSCDGYTNSI YTISISSTAE SGKKPWYLEE 
       360        370        380        390        400
CSSTLATTYS SGESYDKKII TTDLRQRCTD NHTGTSASAP MAAGIIALAL 
       410        420        430        440        450
EANPFLTWRD VQHVIVRTSR AGHLNANDWK TNAAGFKVSH LYGFGLMDAE 
       460        470        480        490        500
AMVMEAEKWT TVPRQHVCVE STDRQIKTIR PNSAVRSIYK ASGCSDNPNR 
       510        520        530        540        550
HVNYLEHVVV RITITHPRRG DLAIYLTSPS GTRSQLLANR LFDHSMEGFK 
       560        570        580        590        600
NWEFMTIHCW GERAAGDWVL EVYDTPSQLR NFKTPGKLKE WSLVLYGTSV 
       610        620        630        640        650
QPYSPTNEFP KVERFRYSRV EDPTDDYGTE DYAGPCDPEC SEVGCDGPGP 
       660        670        680        690        700
DHCNDCLHYY YKLKNNTRIC VSSCPPGHYH ADKKRCRKCA PNCESCFGSH 
       710        720        730        740        750
GDQCMSCKYG YFLNEETNSC VTHCPDGSYQ DTKKNLCRKC SENCKTCTEF 
       760        770        780        790        800
HNCTECRDGL SLQGSRCSVS CEDGRYFNGQ DCQPCHRFCA TCAGAGADGC 
       810        820        830        840        850
INCTEGYFME DGRCVQSCSI SYYFDHSSEN GYKSCKKCDI SCLTCNGPGF 
       860        870        880        890        900
KNCTSCPSGY LLDLGMCQMG AICKDGEYVD EHGHCQTCEA SCAKCQGPTQ 
       910        920        930        940        950
EDCTTCPMTR IFDDGRCVSN CPSWKFEFEN QCHPCHHTCQ RCQGSGPTHC 
       960        970        980        990       1000
TSCGADNYGR EHFLYQGECG DSCPEGHYAT EGNTCLPCPD NCELCHSVHV 
      1010       1020       1030       1040       1050
CTRCMKGYFI APTNHTCQKL ECGQGEVQDP DYEECVPCEE GCLGCSLDDP 
      1060       1070       1080       1090       1100
GTCTSCAMGY YRFDHHCYKT CPEKTYSEEV ECKACDSNCG SCDQNGCYWC 
      1110       1120       1130       1140       1150
EEGFFLLGGS CVRKCGPGFY GDQEMGECES CHRACETCTG PGHDECSSCQ 
      1160       1170       1180       1190       1200
EGLQLLRGMC VHATKTQEEG KFWNDILRKL QPCHSSCKTC NGSATLCTSC 
      1210       1220       1230       1240       1250
PKGAYLLAQA CVSSCPQGTW PSVRSGSCEN CTEACAICSG ADLCKKCQMQ 
      1260       1270       1280       1290       1300
PGHPLFLHEG RCYSKCPEGS YAEDGICERC SSPCRTCEGN ATNCHSCEGG 
      1310       1320       1330       1340       1350
HVLHHGVCQE NCPERHVAVK GVCKHCPEMC QDCIHEKTCK ECTPEFFLHD 
      1360       1370       1380       1390       1400
DMCHQSCPRG FYADSRHCVP CHKDCLECSG PKADDCELCL ESSWVLYDGL 
      1410       1420       1430       1440       1450
CLEECPAGTY YEKETKECRD CHKSCLTCSS SGTCTTCQKG LIMNPRGSCM 
      1460       1470       1480       1490       1500
ANEKCSPSEY WDEDAPGCKP CHVKCFHCMG PAEDQCQTCP MNSLLLNTTC 
      1510       1520       1530       1540       1550
VKDCPEGYYA DEDSNRCAHC HSSCRTCEGR HSRQCHSCRP GWFQLGKECL 
      1560       1570       1580       1590       1600
LQCREGYYAD NSTGRCERCN RSCKGCQGPR PTDCLSCDRF FFLLRSKGEC 
      1610       1620       1630       1640       1650
HRSCPDHYYV EQSTQTCERC HPTCDQCKGK GALNCLSCVW SYHLMGGICT 
      1660       1670       1680       1690       1700
SDCLVGEYRV GEGEKFNCEK CHESCMECKG PGAKNCTLCP ANLVLHMDDS 
      1710       1720       1730       1740       1750
HCLHCCNTSD PPSAQECCDC QDTTDECILR TSKVRPATEH FKTALFITSS 
      1760       1770       1780       1790       1800
MMLVLLLGAA VVVWKKSRGR VQPAAKAGYE KLADPNKSYS SYKSSYREST 
      1810       1820       1830       1840       1850
SFEEDQVIEY RDRDYDEDDD DDIVYMGQDG TVYRKFKYGL LDDDDIDELE 
      1860
YDDESYSYYQ                                             

        10         20         30         40         50
MGWGSRCCCP GRLDLLCVLA LLGGCLLPVC RTRVYTNHWA VKIAGGFPEA 
        60         70         80         90        100
NRIASKYGFI NIGQIGALKD YYHFYHSRTI KRSVISSRGT HSFISMEPKV 
       110        120        130        140        150
EWIQQQVVKK RTKRDYDFSR AQSTYFNDPK WPSMWYMHCS DNTHPCQSDM 
       160        170        180        190        200
NIEGAWKRGY TGKNIVVTIL DDGIERTHPD LMQNYDALAS CDVNGNDLDP 
       210        220        230        240        250
MPRYDASNEN KHGTRCAGEV AAAANNSHCT VGIAFNAKIG GVRMLDGDVT 
       260        270        280        290        300
DMVEAKSVSF NPQHVHIYSA SWGPDDDGKT VDGPAPLTRQ AFENGVRMGR 
       310        320        330        340        350
RGLGSVFVWA SGNGGRSKDH CSCDGYTNSI YTISISSTAE SGKKPWYLEE 
       360        370        380        390        400
CSSTLATTYS SGESYDKKII TTDLRQRCTD NHTGTSASAP MAAGIIALAL 
       410        420        430        440        450
EANPFLTWRD VQHVIVRTSR AGHLNANDWK TNAAGFKVSH LYGFGLMDAE 
       460        470        480        490        500
AMVMEAEKWT TVPRQHVCVE STDRQIKTIR PNSAVRSIYK ASGCSDNPNR 
       510        520        530        540        550
HVNYLEHVVV RITITHPRRG DLAIYLTSPS GTRSQLLANR LFDHSMEGFK 
       560        570        580        590        600
NWEFMTIHCW GERAAGDWVL EVYDTPSQLR NFKTPGKLKE WSLVLYGTSV 
       610        620        630        640        650
QPYSPTNEFP KVERFRYSRV EDPTDDYGTE DYAGPCDPEC SEVGCDGPGP 
       660        670        680        690        700
DHCNDCLHYY YKLKNNTRIC VSSCPPGHYH ADKKRCRKCA PNCESCFGSH 
       710        720        730        740        750
GDQCMSCKYG YFLNEETNSC VTHCPDGSYQ DTKKNLCRKC SENCKTCTEF 
       760        770        780        790        800
HNCTECRDGL SLQGSRCSVS CEDGRYFNGQ DCQPCHRFCA TCAGAGADGC 
       810        820        830        840        850
INCTEGYFME DGRCVQSCSI SYYFDHSSEN GYKSCKKCDI SCLTCNGPGF 
       860        870        880        890        900
KNCTSCPSGY LLDLGMCQMG AICKDATEES WAEGGFCMLV KKNNLCQRKV 
       910 
LQQLCCKTCT FQG                                         

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
2. SIMILARITY comments
   Index of protein domains and families
3. Human chromosome 9
   Human chromosome 9: entries, gene names and cross-references to MIM
4. Peptidase families
   Classification of peptidase families and list of entries