PCSK7_RAT
ID PCSK7_RAT Reviewed; 783 AA.
AC Q62849;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Short=rPC7;
DE AltName: Full=Subtilisin/kexin-like protease PC7;
DE Flags: Precursor;
GN Name=Pcsk7; Synonyms=Pc7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pheochromocytoma, and Spleen;
RX PubMed=8622945; DOI=10.1073/pnas.93.8.3388;
RA Seidah N.G., Hamelin J., Mamarbachi M., Dong W., Tadros H., Mbikay M.,
RA Chretien M., Day R.;
RT "cDNA structure, tissue distribution, and chromosomal localization of rat
RT PC7, a novel mammalian proprotein convertase closest to yeast kexin-like
RT proteinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3388-3393(1996).
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;
CC -!- ACTIVITY REGULATION: Inhibited by zinc and copper.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Single-pass type I membrane protein. Note=Seems to be localized
CC intracellularly to the trans Golgi network.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in colon and
CC spleen. {ECO:0000269|PubMed:8622945}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; U36580; AAB39919.1; -; mRNA.
DR PIR; JC6136; JC6136.
DR RefSeq; NP_062119.1; NM_019246.1.
DR AlphaFoldDB; Q62849; -.
DR SMR; Q62849; -.
DR DIP; DIP-29905N; -.
DR IntAct; Q62849; 1.
DR STRING; 10116.ENSRNOP00000023677; -.
DR MEROPS; S08.077; -.
DR GlyGen; Q62849; 4 sites.
DR iPTMnet; Q62849; -.
DR PhosphoSitePlus; Q62849; -.
DR PaxDb; Q62849; -.
DR PRIDE; Q62849; -.
DR DNASU; 29606; -.
DR Ensembl; ENSRNOT00000023677; ENSRNOP00000023677; ENSRNOG00000017478.
DR GeneID; 29606; -.
DR KEGG; rno:29606; -.
DR UCSC; RGD:3275; rat.
DR CTD; 9159; -.
DR RGD; 3275; Pcsk7.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000157676; -.
DR HOGENOM; CLU_002976_4_3_1; -.
DR InParanoid; Q62849; -.
DR OMA; SFTIFWT; -.
DR OrthoDB; 473018at2759; -.
DR PhylomeDB; Q62849; -.
DR TreeFam; TF314277; -.
DR BRENDA; 3.4.21.B27; 5301.
DR PRO; PR:Q62849; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000017478; Expressed in colon and 18 other tissues.
DR Genevisible; Q62849; RN.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISO:RGD.
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:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..36
FT PROPEP 37..140
FT /id="PRO_0000027118"
FT CHAIN 141..783
FT /note="Proprotein convertase subtilisin/kexin type 7"
FT /id="PRO_0000027119"
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..783
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 REGION 761..783
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 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"
SQ SEQUENCE 783 AA; 85599 MW; 595E159819F5E653 CRC64;
MPKGRQKVPR LDARLGLPIC LCLELAIFFL VPQVMGLTEA GGLDTLGAGG LSWAVHLDSL
EGERKEESLI QQANAVAQAA GLVNAGRIGE LQGHYLFVQP AGHGQAMEAE AMRQQAEAVL
AKHEAVRWHS EQRLLKRAKR 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 QHIIVFTATQ YEDHRADWLT NEAGFSHSHQ HGFGLLNAWR LVNAAKIWTS
VPYLASYVSP MLKENKAVPR SPHSLEVLWN VSRTDLEMSG LKTLEHVAVT VSITHPRRGS
LELKLFCPSG MMSLIGAPRS MDSDPNGFND WTFSTVRCWG ERARGVYRLV IRDVGDEPLQ
VGILQQWQLT LYGSTWSPVD IKDRQSLLES AMSGKYLHDD FTLPCPPGLK IPEEDGYSIT
PNTLKTLVLV GCFSVFWTIY YMLEVCLSQR SKASTHGCRR GCCPWPPQSQ NSKEVGTALE
SMPLCSSKDL DGVDSEHGDC TTASSLLAPE LLGEADWSLS QNSKSDLDCP PHQPPDLKDG
QIC
