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Proprotein convertase subtilisin/kexin type 7 (EC 3.4.21.-) (Lymphoma proprotein convertase) (Prohormone convertase 7) (Proprotein convertase 7) (PC7) (Proprotein convertase 8) (PC8) (hPC8) (Subtilisin/kexin-like protease PC7)

 PCSK7_HUMAN             Reviewed;         785 AA.
Q16549; B0YJ60; Q3C1X1; Q53GM4; Q96FK8; Q9UL57;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
20-JUN-2018, entry version 178.
RecName: Full=Proprotein convertase subtilisin/kexin type 7;
EC=3.4.21.-;
AltName: Full=Lymphoma proprotein convertase;
AltName: Full=Prohormone convertase 7;
AltName: Full=Proprotein convertase 7;
Short=PC7;
AltName: Full=Proprotein convertase 8;
Short=PC8;
Short=hPC8;
AltName: Full=Subtilisin/kexin-like protease PC7;
Flags: Precursor;
Name=PCSK7; Synonyms=LPC, PC7, PC8, SPC7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung carcinoma;
PubMed=8615762; DOI=10.1042/bj3140727;
Bruzzaniti A., Goodge K., Jay P., Taviaux S.A., Lam M.H.C., Berta P.,
Martin T.J., Moseley J.M., Gillespie M.T.;
"PC8, a new member of the convertase family.";
Biochem. J. 314:727-731(1996).
[2]
ERRATUM.
Bruzzaniti A., Goodge K., Jay P., Taviaux S.A., Lam M.H.C., Berta P.,
Martin T.J., Moseley J.M., Gillespie M.T.;
Biochem. J. 316:1007-1007(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell lymphoma;
PubMed=8564950;
Meerabux J., Yaspo M.-L., Roebroek A.J.M., Van de Ven W.J.M.,
Lister T.A., Young B.D.;
"A new member of the proprotein convertase gene family (LPC) is
located at a chromosome translocation breakpoint in lymphomas.";
Cancer Res. 56:448-451(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 527-785.
PubMed=10362256; DOI=10.1038/sj.onc.1202645;
Lecointe N., Meerabux J., Ebihara M., Hill A., Young B.D.;
"Molecular analysis of an unstable genomic region at chromosome band
11q23 reveals a disruption of the gene encoding the alpha2 subunit of
platelet-activating factor acetylhydrolase (Pafah1a2) in human
lymphoma.";
Oncogene 18:2852-2859(1999).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 574-655.
Totoki Y., Yada T., Sakaki Y., Takeda T.;
"Identification of novel human genes predicted by combining multiple
gene-finders.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[12]
GLYCOSYLATION, AND PALMITOYLATION.
PubMed=9341152; DOI=10.1074/jbc.272.43.27116;
Van de Loo J.-W.H.P., Creemers J.W.M., Bright N.A., Young B.D.,
Roebroek A.J.M., Van de Ven W.J.M.;
"Biosynthesis, distinct post-translational modifications, and
functional characterization of lymphoma proprotein convertase.";
J. Biol. Chem. 272:27116-27123(1997).
-!- FUNCTION: Serine endoprotease that processes various proproteins
by cleavage at paired basic amino acids, recognizing the RXXX[KR]R
consensus motif. Likely functions in the constitutive secretory
pathway.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by zinc and copper. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000250}; Single-pass type I membrane protein
{ECO:0000250}. Note=Seems to be localized intracellularly to the
trans Golgi network. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis,
ovary, small intestine, colon and peripheral blood leukocyte.
-!- PTM: Cysteine residues in the cytoplasmic tail are probably
palmitoylated. {ECO:0000269|PubMed:9341152}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9341152}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U40623; AAC50417.1; -; mRNA.
EMBL; U33849; AAB03087.1; -; mRNA.
EMBL; BT006870; AAP35516.1; -; mRNA.
EMBL; AK312429; BAG35338.1; -; mRNA.
EMBL; AK222907; BAD96627.1; -; mRNA.
EMBL; EF445005; ACA06036.1; -; Genomic_DNA.
EMBL; EF445005; ACA06037.1; -; Genomic_DNA.
EMBL; CH471065; EAW67305.1; -; Genomic_DNA.
EMBL; BC010696; AAH10696.1; -; mRNA.
EMBL; AF057710; AAD55137.1; -; Genomic_DNA.
EMBL; AB231710; BAE46876.1; -; mRNA.
CCDS; CCDS8382.1; -.
PIR; S64706; S64706.
RefSeq; NP_004707.2; NM_004716.3.
UniGene; Hs.648612; -.
ProteinModelPortal; Q16549; -.
SMR; Q16549; -.
BioGrid; 114604; 1.
IntAct; Q16549; 1.
MINT; Q16549; -.
STRING; 9606.ENSP00000325917; -.
BindingDB; Q16549; -.
ChEMBL; CHEMBL2232; -.
GuidetoPHARMACOLOGY; 2387; -.
MEROPS; S08.077; -.
iPTMnet; Q16549; -.
PhosphoSitePlus; Q16549; -.
SwissPalm; Q16549; -.
BioMuta; PCSK7; -.
DMDM; 205830663; -.
PaxDb; Q16549; -.
PeptideAtlas; Q16549; -.
PRIDE; Q16549; -.
ProteomicsDB; 60909; -.
DNASU; 9159; -.
Ensembl; ENST00000320934; ENSP00000325917; ENSG00000160613.
GeneID; 9159; -.
KEGG; hsa:9159; -.
UCSC; uc001pqr.4; human.
CTD; 9159; -.
DisGeNET; 9159; -.
EuPathDB; HostDB:ENSG00000160613.12; -.
GeneCards; PCSK7; -.
H-InvDB; HIX0026164; -.
H-InvDB; HIX0191666; -.
HGNC; HGNC:8748; PCSK7.
HPA; HPA043181; -.
HPA; HPA052957; -.
MIM; 604872; gene.
neXtProt; NX_Q16549; -.
OpenTargets; ENSG00000160613; -.
PharmGKB; PA33094; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; Q16549; -.
KO; K08673; -.
OMA; EVLWNVS; -.
OrthoDB; EOG091G01XU; -.
PhylomeDB; Q16549; -.
TreeFam; TF314277; -.
BRENDA; 3.4.21.B27; 2681.
SignaLink; Q16549; -.
SIGNOR; Q16549; -.
ChiTaRS; PCSK7; human.
GeneWiki; PCSK7; -.
GenomeRNAi; 9159; -.
PRO; PR:Q16549; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000160613; -.
CleanEx; HS_PCSK7; -.
ExpressionAtlas; Q16549; baseline and differential.
Genevisible; Q16549; HS.
GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0016486; P:peptide hormone processing; NAS:UniProtKB.
GO; GO:0016485; P:protein processing; IDA:MGI.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.30.70.850; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR002884; P_dom.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR032815; S8_pro-domain.
InterPro; IPR038466; S8_pro-domain_sf.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Glycoprotein;
Golgi apparatus; Hydrolase; Lipoprotein; Membrane; Palmitate;
Polymorphism; Protease; Reference proteome; Serine protease; Signal;
Transmembrane; Transmembrane helix; Zymogen.
SIGNAL 1 37 {ECO:0000250}.
PROPEP 38 141 {ECO:0000250}.
/FTId=PRO_0000027114.
CHAIN 142 785 Proprotein convertase subtilisin/kexin
type 7.
/FTId=PRO_0000027115.
TOPO_DOM 142 667 Extracellular. {ECO:0000255}.
TRANSMEM 668 688 Helical. {ECO:0000255}.
TOPO_DOM 689 785 Cytoplasmic. {ECO:0000255}.
DOMAIN 182 474 Peptidase S8.
DOMAIN 481 618 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
ACT_SITE 187 187 Charge relay system. {ECO:0000250}.
ACT_SITE 228 228 Charge relay system. {ECO:0000250}.
ACT_SITE 406 406 Charge relay system. {ECO:0000250}.
SITE 141 142 Cleavage; by autolysis. {ECO:0000250}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 511 511 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 688 688 L -> V (in dbSNP:rs608620).
/FTId=VAR_044419.
VARIANT 689 689 S -> N (in dbSNP:rs45539233).
/FTId=VAR_044420.
VARIANT 700 700 R -> M (in dbSNP:rs45574931).
/FTId=VAR_044421.
VARIANT 708 708 H -> Y (in dbSNP:rs473131).
/FTId=VAR_044422.
VARIANT 711 711 R -> Q (in dbSNP:rs473093).
/FTId=VAR_044423.
CONFLICT 52 52 P -> A (in Ref. 1; AAC50417 and 3;
AAB03087). {ECO:0000305}.
CONFLICT 112 112 A -> P (in Ref. 1; AAC50417 and 3;
AAB03087). {ECO:0000305}.
CONFLICT 228 228 H -> R (in Ref. 6; BAD96627).
{ECO:0000305}.
CONFLICT 353 353 A -> T (in Ref. 7; ACA06037).
{ECO:0000305}.
SEQUENCE 785 AA; 86247 MW; 4A268754766C32DA CRC64;
MPKGRQKVPH LDAPLGLPTC LWLELAGLFL LVPWVMGLAG TGGPDGQGTG GPSWAVHLES
LEGDGEEETL EQQADALAQA AGLVNAGRIG ELQGHYLFVQ PAGHRPALEV EAIRQQVEAV
LAGHEAVRWH SEQRLLRRAK RSVHFNDPKY PQQWHLNNRR SPGRDINVTG VWERNVTGRG
VTVVVVDDGV EHTIQDIAPN YSPEGSYDLN SNDPDPMPHP DVENGNHHGT RCAGEIAAVP
NNSFCAVGVA YGSRIAGIRV LDGPLTDSME AVAFNKHYQI NDIYSCSWGP DDDGKTVDGP
HQLGKAALQH GVIAGRQGFG SIFVVASGNG GQHNDNCNYD GYANSIYTVT IGAVDEEGRM
PFYAEECASM LAVTFSGGDK MLRSIVTTDW DLQKGTGCTE GHTGTSAAAP LAAGMIALML
QVRPCLTWRD VQHIIVFTAT RYEDRRAEWV TNEAGFSHSH QHGFGLLNAW RLVNAAKIWT
SVPYLASYVS PVLKENKAIP QSPRSLEVLW NVSRMDLEMS GLKTLEHVAV TVSITHPRRG
SLELKLFCPS GMMSLIGAPR SMDSDPNGFN DWTFSTVRCW GERARGTYRL VIRDVGDESF
QVGILRQWQL TLYGSVWSAV DIRDRQRLLE SAMSGKYLHD DFALPCPPGL KIPEEDGYTI
TPNTLKTLVL VGCFTVFWTV YYMLEVYLSQ RNVASNQVCR SGPCHWPHRS RKAKEEGTEL
ESVPLCSSKD PDEVETESRG PPTTSDLLAP DLLEQGDWSL SQNKSALDCP HQHLDVPHGK
EEQIC


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