PCSK7_MOUSE
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 03-AUG-2022, entry version 180.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 GlyGen; Q61139; 4 sites.
DR iPTMnet; Q61139; -.
DR PhosphoSitePlus; Q61139; -.
DR PaxDb; Q61139; -.
DR PRIDE; Q61139; -.
DR ProteomicsDB; 288002; -.
DR Antibodypedia; 32336; 153 antibodies from 23 providers.
DR DNASU; 18554; -.
DR Ensembl; ENSMUST00000039059; ENSMUSP00000047508; ENSMUSG00000035382.
DR Ensembl; ENSMUST00000216672; ENSMUSP00000150393; ENSMUSG00000035382.
DR GeneID; 18554; -.
DR KEGG; mmu:18554; -.
DR UCSC; uc009pgp.1; mouse.
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; SFTIFWT; -.
DR OrthoDB; 473018at2759; -.
DR PhylomeDB; Q61139; -.
DR TreeFam; TF314277; -.
DR BRENDA; 3.4.21.B27; 3474.
DR BioGRID-ORCS; 18554; 4 hits in 75 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 222 other tissues.
DR ExpressionAtlas; Q61139; baseline and differential.
DR Genevisible; Q61139; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0030173; C:integral component of 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; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 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 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; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 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.
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
