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Q92824 (PCSK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proprotein convertase subtilisin/kexin type 5

EC=3.4.21.-
Alternative name(s):
Proprotein convertase 5
Short name=PC5
Proprotein convertase 6
Short name=PC6
Short name=hPC6
Subtilisin/kexin-like protease PC5
Gene names
Name:PCSK5
Synonyms:PC5, PC6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1860 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Likely to represent a widespread endoprotease activity within the constitutive and regulated secretory pathway. Capable of cleavage at the RX(K/R)R consensus motif. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha-integrins. Ref.9 Ref.10 Ref.11

Catalytic activity

Release of mature proteins from their proproteins by cleavage of Arg-Xaa-Yaa-Arg-|-Zaa bonds, where Xaa can be any amino acid and Yaa is Arg or Lys.

Subcellular location

Isoform PC6A: Secreted. Note: Secreted through the regulated secretory pathway By similarity.

Isoform PC6B: Endomembrane system; Single-pass type I membrane protein. Note: Type I membrane protein localized to a paranuclear post-Golgi network compartment in communication with early endosomes By similarity.

Tissue specificity

Expressed in T-lymphocytes.

Domain

The propeptide domain acts as an intramolecular chaperone assisting the folding of the zymogen within the endoplasmic reticulum.

AC 1 and AC 2 (clusters of acidic amino acids) contain sorting information. AC 1 directs TGN localization and interacts with the TGN sorting protein PACS-1 By similarity.

Sequence similarities

Belongs to the peptidase S8 family.

Contains 1 homo B/P domain.

Contains 1 PLAC domain.

Ontologies

Keywords
   Biological processPregnancy
   Cellular componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from mutant phenotype PubMed 18519639. Source: BHF-UCL

cell-cell signaling

Traceable author statement PubMed 8901832. Source: ProtInc

cytokine biosynthetic process

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

embryo implantation

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

embryonic digestive tract development

Inferred from mutant phenotype PubMed 18519639. Source: BHF-UCL

embryonic skeletal system development

Inferred from mutant phenotype PubMed 18519639. Source: BHF-UCL

heart development

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

kidney development

Inferred from mutant phenotype PubMed 18519639. Source: BHF-UCL

limb morphogenesis

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

nerve growth factor processing

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptide biosynthetic process

Inferred from direct assay PubMed 8901832. Source: BHF-UCL

peptide hormone processing

Inferred from direct assay PubMed 8901832. Source: BHF-UCL

protein processing

Inferred from direct assay PubMed 8901832. Source: BHF-UCL

renin secretion into blood stream

Inferred from expression pattern PubMed 8901832. Source: BHF-UCL

respiratory tube development

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

signal peptide processing

Inferred from direct assay PubMed 16912035. Source: HGNC

viral life cycle

Inferred from expression pattern PubMed 8940009. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: BHF-UCL

Golgi lumen

Traceable author statement. Source: Reactome

extracellular space

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

secretory granule

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionpeptidase activity

Inferred from direct assay PubMed 15606899. Source: MGI

peptide binding

Inferred from sequence or structural similarity PubMed 8940009. Source: BHF-UCL

serine-type endopeptidase activity

Inferred from direct assay PubMed 8901832. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform PC6B (identifier: Q92824-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform PC6A (identifier: Q92824-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     876-913: GEYVDEHGHC...TTCPMTRIFD → ATEESWAEGG...LCCKTCTFQG
     914-1860: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Propeptide33 – 11482 By similarity
PRO_0000027102
Chain115 – 18601746Proprotein convertase subtilisin/kexin type 5
PRO_0000027103

Regions

Topological domain115 – 17431629Extracellular Potential
Transmembrane1744 – 176421Helical; Potential
Topological domain1765 – 186096Cytoplasmic Potential
Domain462 – 600139Homo B/P
Domain869 – 91345PLAC
Region115 – 454340Catalytic
Region636 – 17271092CRM (Cys-rich motif)
Region1807 – 182620AC 1 By similarity
Region1838 – 186023AC 2 By similarity
Motif519 – 5213Cell attachment site Potential

Sites

Active site1711Charge relay system By similarity
Active site2121Charge relay system By similarity
Active site3861Charge relay system By similarity
Site114 – 1152Cleavage; by autolysis By similarity

Amino acid modifications

Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential
Glycosylation7521N-linked (GlcNAc...) Potential
Glycosylation8021N-linked (GlcNAc...) Potential
Glycosylation8521N-linked (GlcNAc...) Potential
Glycosylation10141N-linked (GlcNAc...) Potential
Glycosylation11911N-linked (GlcNAc...) Potential
Glycosylation12901N-linked (GlcNAc...) Potential
Glycosylation14971N-linked (GlcNAc...) Potential
Glycosylation16851N-linked (GlcNAc...) Potential
Glycosylation17071N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence876 – 91338GEYVD…TRIFD → ATEESWAEGGFCMLVKKNNL CQRKVLQQLCCKTCTFQG in isoform PC6A.
VSP_042017
Alternative sequence914 – 1860947Missing in isoform PC6A.
VSP_042018

Experimental info

Sequence conflict21G → D in AAC50643. Ref.1
Sequence conflict41G → E in AAC50643. Ref.1
Sequence conflict1181F → S in AAC50643. Ref.1
Sequence conflict1211A → V in AAC50643. Ref.1
Sequence conflict5111R → A in AAA91807. Ref.7
Sequence conflict6011Q → R in AAC50643. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform PC6B (Long) [UniParc].

Last modified November 16, 2011. Version 4.
Checksum: 96B3E7C8215BCC85

FASTA1,860206,942
        10         20         30         40         50         60 
MGWGSRCCCP GRLDLLCVLA LLGGCLLPVC RTRVYTNHWA VKIAGGFPEA NRIASKYGFI 

        70         80         90        100        110        120 
NIGQIGALKD YYHFYHSRTI KRSVISSRGT HSFISMEPKV EWIQQQVVKK RTKRDYDFSR 

       130        140        150        160        170        180 
AQSTYFNDPK WPSMWYMHCS DNTHPCQSDM NIEGAWKRGY TGKNIVVTIL DDGIERTHPD 

       190        200        210        220        230        240 
LMQNYDALAS CDVNGNDLDP MPRYDASNEN KHGTRCAGEV AAAANNSHCT VGIAFNAKIG 

       250        260        270        280        290        300 
GVRMLDGDVT DMVEAKSVSF NPQHVHIYSA SWGPDDDGKT VDGPAPLTRQ AFENGVRMGR 

       310        320        330        340        350        360 
RGLGSVFVWA SGNGGRSKDH CSCDGYTNSI YTISISSTAE SGKKPWYLEE CSSTLATTYS 

       370        380        390        400        410        420 
SGESYDKKII TTDLRQRCTD NHTGTSASAP MAAGIIALAL EANPFLTWRD VQHVIVRTSR 

       430        440        450        460        470        480 
AGHLNANDWK TNAAGFKVSH LYGFGLMDAE AMVMEAEKWT TVPRQHVCVE STDRQIKTIR 

       490        500        510        520        530        540 
PNSAVRSIYK ASGCSDNPNR HVNYLEHVVV RITITHPRRG DLAIYLTSPS GTRSQLLANR 

       550        560        570        580        590        600 
LFDHSMEGFK NWEFMTIHCW GERAAGDWVL EVYDTPSQLR NFKTPGKLKE WSLVLYGTSV 

       610        620        630        640        650        660 
QPYSPTNEFP KVERFRYSRV EDPTDDYGTE DYAGPCDPEC SEVGCDGPGP DHCNDCLHYY 

       670        680        690        700        710        720 
YKLKNNTRIC VSSCPPGHYH ADKKRCRKCA PNCESCFGSH GDQCMSCKYG YFLNEETNSC 

       730        740        750        760        770        780 
VTHCPDGSYQ DTKKNLCRKC SENCKTCTEF HNCTECRDGL SLQGSRCSVS CEDGRYFNGQ 

       790        800        810        820        830        840 
DCQPCHRFCA TCAGAGADGC INCTEGYFME DGRCVQSCSI SYYFDHSSEN GYKSCKKCDI 

       850        860        870        880        890        900 
SCLTCNGPGF KNCTSCPSGY LLDLGMCQMG AICKDGEYVD EHGHCQTCEA SCAKCQGPTQ 

       910        920        930        940        950        960 
EDCTTCPMTR IFDDGRCVSN CPSWKFEFEN QCHPCHHTCQ RCQGSGPTHC TSCGADNYGR 

       970        980        990       1000       1010       1020 
EHFLYQGECG DSCPEGHYAT EGNTCLPCPD NCELCHSVHV CTRCMKGYFI APTNHTCQKL 

      1030       1040       1050       1060       1070       1080 
ECGQGEVQDP DYEECVPCEE GCLGCSLDDP GTCTSCAMGY YRFDHHCYKT CPEKTYSEEV 

      1090       1100       1110       1120       1130       1140 
ECKACDSNCG SCDQNGCYWC EEGFFLLGGS CVRKCGPGFY GDQEMGECES CHRACETCTG 

      1150       1160       1170       1180       1190       1200 
PGHDECSSCQ EGLQLLRGMC VHATKTQEEG KFWNDILRKL QPCHSSCKTC NGSATLCTSC 

      1210       1220       1230       1240       1250       1260 
PKGAYLLAQA CVSSCPQGTW PSVRSGSCEN CTEACAICSG ADLCKKCQMQ PGHPLFLHEG 

      1270       1280       1290       1300       1310       1320 
RCYSKCPEGS YAEDGICERC SSPCRTCEGN ATNCHSCEGG HVLHHGVCQE NCPERHVAVK 

      1330       1340       1350       1360       1370       1380 
GVCKHCPEMC QDCIHEKTCK ECTPEFFLHD DMCHQSCPRG FYADSRHCVP CHKDCLECSG 

      1390       1400       1410       1420       1430       1440 
PKADDCELCL ESSWVLYDGL CLEECPAGTY YEKETKECRD CHKSCLTCSS SGTCTTCQKG 

      1450       1460       1470       1480       1490       1500 
LIMNPRGSCM ANEKCSPSEY WDEDAPGCKP CHVKCFHCMG PAEDQCQTCP MNSLLLNTTC 

      1510       1520       1530       1540       1550       1560 
VKDCPEGYYA DEDSNRCAHC HSSCRTCEGR HSRQCHSCRP GWFQLGKECL LQCREGYYAD 

      1570       1580       1590       1600       1610       1620 
NSTGRCERCN RSCKGCQGPR PTDCLSCDRF FFLLRSKGEC HRSCPDHYYV EQSTQTCERC 

      1630       1640       1650       1660       1670       1680 
HPTCDQCKGK GALNCLSCVW SYHLMGGICT SDCLVGEYRV GEGEKFNCEK CHESCMECKG 

      1690       1700       1710       1720       1730       1740 
PGAKNCTLCP ANLVLHMDDS HCLHCCNTSD PPSAQECCDC QDTTDECILR TSKVRPATEH 

      1750       1760       1770       1780       1790       1800 
FKTALFITSS MMLVLLLGAA VVVWKKSRGR VQPAAKAGYE KLADPNKSYS SYKSSYREST 

      1810       1820       1830       1840       1850       1860 
SFEEDQVIEY RDRDYDEDDD DDIVYMGQDG TVYRKFKYGL LDDDDIDELE YDDESYSYYQ 

« Hide

Isoform PC6A (Short) [UniParc].

Checksum: 7A2E63EFC49104BC
Show »

FASTA913101,649

References

« Hide 'large scale' references
[1]"Isolation of the human PC6 gene encoding the putative host protease for HIV-1 gp160 processing in CD4+ T lymphocytes."
Miranda L., Wolf J., Pichuantes S., Duke R., Franzusoff A.
Proc. Natl. Acad. Sci. U.S.A. 93:7695-7700(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PC6A), ALTERNATIVE SPLICING.
Tissue: T-cell.
[2]Franzusoff A., Miranda L., Wolf J., Pichuantes S., Lu Y., Duke R.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PC6A).
Tissue: Lymph node.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM PC6A).
Tissue: Kidney.
[7]Reudelhuber T.L.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-913 (ISOFORM PC6A).
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1166-1860 (ISOFORM PC6B).
Tissue: Tongue.
[9]"Proteomic identification of caldesmon as a physiological substrate of proprotein convertase 6 in human uterine decidual cells essential for pregnancy establishment."
Kilpatrick L.M., Stephens A.N., Hardman B.M., Salamonsen L.A., Li Y., Stanton P.G., Nie G.
J. Proteome Res. 8:4983-4992(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PREGNANCY ESTABLISHMENT.
[10]"Posttranslational activation of bone morphogenetic protein 2 is mediated by proprotein convertase 6 during decidualization for pregnancy establishment."
Heng S., Paule S., Hardman B., Li Y., Singh H., Rainczuk A., Stephens A.N., Nie G.
Endocrinology 151:3909-3917(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PREGNANCY ESTABLISHMENT.
[11]"Cleavage of endometrial alpha-integrins into their functional forms is mediated by proprotein convertase 5/6."
Paule S., Aljofan M., Simon C., Rombauts L.J., Nie G.
Hum. Reprod. 27:2766-2774(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U56387 mRNA. Translation: AAC50643.2.
AL834522 mRNA. Translation: CAD39178.1.
AL359253, AL353607 Genomic DNA. Translation: CAH73743.1.
AL353607, AL359253 Genomic DNA. Translation: CAI41233.1.
AL391868 Genomic DNA. No translation available.
AL589653 Genomic DNA. No translation available.
CH471089 Genomic DNA. Translation: EAW62575.1.
BC012064 mRNA. Translation: AAH12064.1.
U49114 mRNA. Translation: AAA91807.1.
AK122718 mRNA. No translation available.
CCDSCCDS55320.1. [Q92824-1]
CCDS6652.1. [Q92824-2]
PIRG02428.
JC6148.
RefSeqNP_001177411.1. NM_001190482.1. [Q92824-1]
NP_006191.2. NM_006200.5. [Q92824-2]
UniGeneHs.368542.

3D structure databases

ProteinModelPortalQ92824.
SMRQ92824. Positions 128-599.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111152. 7 interactions.
IntActQ92824. 4 interactions.
MINTMINT-1474189.
STRING9606.ENSP00000365943.

Chemistry

BindingDBQ92824.
ChEMBLCHEMBL2826.

Protein family/group databases

MEROPSS08.076.

PTM databases

PhosphoSiteQ92824.

Polymorphism databases

DMDM357529585.

Proteomic databases

PaxDbQ92824.
PRIDEQ92824.

Protocols and materials databases

DNASU5125.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376752; ENSP00000365943; ENSG00000099139. [Q92824-2]
ENST00000545128; ENSP00000446280; ENSG00000099139. [Q92824-1]
GeneID5125.
KEGGhsa:5125.
UCSCuc004ajz.3. human. [Q92824-2]
uc004akc.2. human. [Q92824-1]

Organism-specific databases

CTD5125.
GeneCardsGC09P078505.
HGNCHGNC:8747. PCSK5.
HPAHPA031072.
MIM600488. gene.
neXtProtNX_Q92824.
PharmGKBPA33093.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4935.
HOGENOMHOG000192536.
HOVERGENHBG008705.
KOK08654.
OMALHEGRCY.
PhylomeDBQ92824.
TreeFamTF314277.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ92824.

Gene expression databases

ArrayExpressQ92824.
BgeeQ92824.
CleanExHS_PCSK5.
GenevestigatorQ92824.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProIPR000742. EG-like_dom.
IPR006212. Furin_repeat.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SMARTSM00181. EGF. 1 hit.
SM00261. FU. 22 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
SSF57184. SSF57184. 7 hits.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPCSK5.
GenomeRNAi5125.
NextBio19754.
PMAP-CutDBQ92824.
PROQ92824.
SOURCESearch...

Entry information

Entry namePCSK5_HUMAN
AccessionPrimary (citable) accession number: Q92824
Secondary accession number(s): F5H2G7, Q13527, Q96EP4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 16, 2011
Last modified: July 9, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM