ID   PCSK7_MOUSE             Reviewed;         770 AA.
AC   Q61139; O08577; Q922W4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Proprotein convertase subtilisin/kexin type 7;
DE            EC=3.4.21.-;
DE   AltName: Full=Prohormone convertase 7;
DE   AltName: Full=Proprotein convertase 7;
DE            Short=PC7;
DE   AltName: Full=Subtilisin-like proprotein convertase 7;
DE            Short=SPC7;
DE   AltName: Full=Subtilisin/kexin-like protease PC7;
DE   Flags: Precursor;
GN   Name=Pcsk7; Synonyms=Pc7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=8698813; DOI=10.1083/jcb.134.1.181;
RA   Constam D.B., Calfon M., Robertson E.J.;
RT   "SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone
RT   morphogenetic proteins at distinct sites during embryogenesis.";
RL   J. Cell Biol. 134:181-191(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-384.
RA   Ebihara M., Meerabux J., Young B.D.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine endoprotease that processes various proproteins by
CC       cleavage at paired basic amino acids, recognizing the RXXX[KR]R
CC       consensus motif. Likely functions in the constitutive secretory
CC       pathway.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by zinc and copper. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Note=Seems to be localized intracellularly to the trans Golgi network.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, lung, muscle,
CC       heart, liver, kidney, spleen and thymus.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at constitutive levels
CC       during embryogenesis. {ECO:0000269|PubMed:8698813}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; U48830; AAB09725.1; -; mRNA.
DR   EMBL; AK148416; BAE28541.1; -; mRNA.
DR   EMBL; AK165389; BAE38156.1; -; mRNA.
DR   EMBL; CH466522; EDL25666.1; -; Genomic_DNA.
DR   EMBL; BC006730; AAH06730.1; -; mRNA.
DR   EMBL; U75902; AAB51126.1; -; Genomic_DNA.
DR   CCDS; CCDS40609.1; -.
DR   RefSeq; NP_001268863.1; NM_001281934.1.
DR   RefSeq; NP_032820.2; NM_008794.2.
DR   RefSeq; XP_017168699.1; XM_017313210.1.
DR   AlphaFoldDB; Q61139; -.
DR   SMR; Q61139; -.
DR   STRING; 10090.ENSMUSP00000047508; -.
DR   MEROPS; S08.077; -.
DR   GlyCosmos; Q61139; 4 sites, No reported glycans.
DR   GlyGen; Q61139; 4 sites.
DR   iPTMnet; Q61139; -.
DR   PhosphoSitePlus; Q61139; -.
DR   PaxDb; 10090-ENSMUSP00000047508; -.
DR   ProteomicsDB; 288002; -.
DR   Antibodypedia; 32336; 161 antibodies from 23 providers.
DR   DNASU; 18554; -.
DR   Ensembl; ENSMUST00000039059.8; ENSMUSP00000047508.7; ENSMUSG00000035382.10.
DR   Ensembl; ENSMUST00000216672.2; ENSMUSP00000150393.2; ENSMUSG00000035382.10.
DR   GeneID; 18554; -.
DR   KEGG; mmu:18554; -.
DR   UCSC; uc009pgp.1; mouse.
DR   AGR; MGI:107421; -.
DR   CTD; 9159; -.
DR   MGI; MGI:107421; Pcsk7.
DR   VEuPathDB; HostDB:ENSMUSG00000035382; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   GeneTree; ENSGT00940000157676; -.
DR   HOGENOM; CLU_002976_4_3_1; -.
DR   InParanoid; Q61139; -.
DR   OMA; NGRMPFY; -.
DR   OrthoDB; 5474719at2759; -.
DR   PhylomeDB; Q61139; -.
DR   TreeFam; TF314277; -.
DR   BRENDA; 3.4.21.B27; 3474.
DR   BioGRID-ORCS; 18554; 4 hits in 80 CRISPR screens.
DR   ChiTaRS; Pcsk7; mouse.
DR   PRO; PR:Q61139; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q61139; Protein.
DR   Bgee; ENSMUSG00000035382; Expressed in granulocyte and 225 other cell types or tissues.
DR   ExpressionAtlas; Q61139; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; ISO:MGI.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   PANTHER; PTHR42884:SF28; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 7; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   Genevisible; Q61139; MM.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Membrane; Protease; Reference proteome; Serine protease; Signal;
KW   Transmembrane; Transmembrane helix; Zymogen.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000250"
FT   PROPEP          37..140
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027116"
FT   CHAIN           141..770
FT                   /note="Proprotein convertase subtilisin/kexin type 7"
FT                   /id="PRO_0000027117"
FT   TOPO_DOM        141..666
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        667..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        688..770
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          152..472
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          480..617
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   REGION          195..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        405
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            140..141
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        191..193
FT                   /note="HTV -> THR (in Ref. 1; AAB09725)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   770 AA;  84358 MW;  E612EB6B7A0E6BFA CRC64;
     MPKGRQKVPH LDAHLGLPIC LWLELAIFFL VPQVMGLSEA GGLDILGTGG LSWAVHLDSL
     EGERKEESLT QQADAVAQAA GLVNAGRIGE LQGHYLFVQP TGHRQAMEVE AMRQQAEAVL
     ARHEAVRWHS EQTLLKRAKR SIHFNDPKYP QQWHLNNRRS PGRDINVTGV WERNVTGRGV
     TVVVVDDGVE HTVQDIAPNY SPEGSYDLNS NDPDPMPHPD EENGNHHGTR CAGEIAAVPN
     NSFCAVGVAY GSRIAGIRVL DGPLTDSMEA VAFNKHYQIN DIYSCSWGPD DDGKTVDGPH
     QLGKAALQHG VMAGRQGFGS IFVVASGNGG QHNDNCNYDG YANSIYTVTI GAVDEEGRMP
     FYAEECASML AVTFSGGDKM LRSIVTTDWD LQKGTGCTEG HTGTSAAAPL AAGMIALMLQ
     VRPCLTWRDV QHIIVFTAIQ YEDHHADWLT NEAGFSHSHQ HGFGLLNAWR LVNAAKIWTS
     VPYLASYVSP MLKENKAVPR SPHSLEVLWN VSRTDLEMSG LKTLEHVAVT VSITHPRRGS
     LELKLFCPSG MMSLIGAPRS MDSDPNGFNA WTFSTVRCWG ERARGVYRLV IRDVGDEPLQ
     MGILQQWQLT LYGSMWSPVD IKDRQSLLES AMSGKYLHDG FTLPCPPGLK IPEEDGYTIT
     PNTLKTLVLV GCFSVFWTIY YMLEVCLSQR NKASTHGCRK GCCPWAPRRQ NSKDAGTALE
     SMPLCSSKDL DGVDSEHGDC TTASSFLAPE LDCPPHQPPD LLQGKSGQIC
//