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Proprotein convertase subtilisin/kexin type 4 (PC4) (EC 3.4.21.-) (KEX2-like endoprotease 3) (Neuroendocrine convertase 3) (NEC 3) (Prohormone convertase 3)

 PCSK4_RAT               Reviewed;         678 AA.
Q78EH2; A1A4C9; Q07213; Q07214;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
20-DEC-2017, entry version 101.
RecName: Full=Proprotein convertase subtilisin/kexin type 4;
Short=PC4;
EC=3.4.21.-;
AltName: Full=KEX2-like endoprotease 3;
AltName: Full=Neuroendocrine convertase 3;
Short=NEC 3;
AltName: Full=Prohormone convertase 3;
Flags: Precursor;
Name=Pcsk4; Synonyms=Nec-3, Nec3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Testis;
PubMed=1448111; DOI=10.1210/mend.6.10.1448111;
Seidah N.G., Day R., Hamelin J., Gaspar A., Collard M.W., Chretien M.;
"Testicular expression of PC4 in the rat: molecular diversity of a
novel germ cell-specific Kex2/subtilisin-like proprotein convertase.";
Mol. Endocrinol. 6:1559-1570(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Testis;
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).
[3]
SUBCELLULAR LOCATION.
PubMed=21080038; DOI=10.1007/s11010-010-0635-y;
Gyamera-Acheampong C., Sirois F., Denis N.J., Mishra P., Figeys D.,
Basak A., Mbikay M.;
"The precursor to the germ cell-specific PCSK4 proteinase is
inefficiently activated in transfected somatic cells: evidence of
interaction with the BiP chaperone.";
Mol. Cell. Biochem. 348:43-52(2011).
-!- FUNCTION: Proprotein convertase involved in the processing of
hormone and other protein precursors at sites comprised of pairs
of basic amino acid residues. In males, important for ADAM2
processing as well as other acrosomal proteins with roles in
fertilization and critical for normal fertilization events such as
sperm capacitation, acrosome reaction and binding of sperm to zona
pellucida (By similarity). Plays also a role in female fertility,
involved in the regulation of trophoblast migration and placental
development, may be through the proteolytical processing and
activation of proteins such as IGF2 (By similarity). May also
participate in folliculogenesis in the ovaries (By similarity).
{ECO:0000250|UniProtKB:P29121, ECO:0000250|UniProtKB:Q6UW60}.
-!- SUBUNIT: The proPCSK4 form interacts with HSPA5; the interaction
takes place at the endoplasmic reticulum.
{ECO:0000250|UniProtKB:Q6UW60}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
acrosome membrane {ECO:0000305|PubMed:21080038}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q78EH2-1; Sequence=Displayed;
Name=2;
IsoId=Q78EH2-2; Sequence=VSP_011273;
Name=3; Synonyms=rPC4-A;
IsoId=Q78EH2-3; Sequence=VSP_011274;
Name=4; Synonyms=rPC4-B;
IsoId=Q78EH2-4; Sequence=VSP_011275;
Name=5; Synonyms=rPC4-C;
IsoId=Q78EH2-5; Sequence=VSP_011276;
-!- TISSUE SPECIFICITY: Expressed abundantly in the testis. High
levels seen in germ cells but not in Leydig, Sertoli or
peritubular cells. Expressed in the pachytene spermatocytes and
the round spermatids but not in the elongating spermatids. May be
expressed within hormonally stimulated ovaries.
{ECO:0000269|PubMed:1448111}.
-!- DEVELOPMENTAL STAGE: First expressed postnatally between days 19
and 22 coinciding with the early stages of spermiogenesis. The
levels increase up to postnatal day 60.
{ECO:0000269|PubMed:1448111}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UW60}.
-!- PTM: Synthesized in the endoplasmic reticulum as a zymogen, is
matured by autocatalytic cleavage between the prodomain and the
catalytic domain. {ECO:0000250|UniProtKB:Q6UW60}.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
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EMBL; L14937; AAA41814.1; -; mRNA.
EMBL; L14937; AAA41815.1; -; mRNA.
EMBL; L14937; AAA41816.1; -; mRNA.
EMBL; BC097288; AAH97288.1; -; mRNA.
PIR; A45357; A45357.
RefSeq; NP_598243.1; NM_133559.1. [Q78EH2-3]
UniGene; Rn.2899; -.
ProteinModelPortal; Q78EH2; -.
SMR; Q78EH2; -.
STRING; 10116.ENSRNOP00000022358; -.
MEROPS; S08.074; -.
PaxDb; Q78EH2; -.
PRIDE; Q78EH2; -.
GeneID; 171085; -.
KEGG; rno:171085; -.
UCSC; RGD:620325; rat. [Q78EH2-1]
CTD; 54760; -.
RGD; 620325; Pcsk4.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; Q78EH2; -.
KO; K08671; -.
PhylomeDB; Q78EH2; -.
BRENDA; 3.4.21.B25; 5301.
PRO; PR:Q78EH2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
GO; GO:0009566; P:fertilization; ISS:UniProtKB.
GO; GO:0016485; P:protein processing; ISS:UniProtKB.
GO; GO:0022414; P:reproductive process; ISS:UniProtKB.
GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR002884; P_dom.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR032815; S8_pro-domain.
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.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
2: Evidence at transcript level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Cytoplasmic vesicle; Glycoprotein; Hydrolase;
Membrane; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 110 {ECO:0000255}.
/FTId=PRO_0000027100.
CHAIN 111 678 Proprotein convertase subtilisin/kexin
type 4.
/FTId=PRO_0000027101.
DOMAIN 150 436 Peptidase S8.
DOMAIN 446 580 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
ACT_SITE 155 155 Charge relay system. {ECO:0000250}.
ACT_SITE 196 196 Charge relay system. {ECO:0000250}.
ACT_SITE 370 370 Charge relay system. {ECO:0000250}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 590 678 ESHCPLSIVAELCLISSKQWWWLYSHTQQPVTKGQDSCHPP
TTPARQLDQRLHCLFPAPHAGSASEPLQGLSPLAAILAISL
GPWCCPC -> VTSCAHACAEGHRGAVPGKSLSPLHCGRTL
PHLQQAVVVALQPHTAASDQGTGQLSPSYHTCSAA (in
isoform 3). {ECO:0000303|PubMed:1448111}.
/FTId=VSP_011274.
VAR_SEQ 590 678 ESHCPLSIVAELCLISSKQWWWLYSHTQQPVTKGQDSCHPP
TTPARQLDQRLHCLFPAPHAGSASEPLQGLSPLAAILAISL
GPWCCPC -> KVIVPSPLWQNSASSPASSGGGSTATHSSQ
(in isoform 4).
{ECO:0000303|PubMed:1448111,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011275.
VAR_SEQ 590 678 ESHCPLSIVAELCLISSKQWWWLYSHTQQPVTKGQDSCHPP
TTPARQLDQRLHCLFPAPHAGSASEPLQGLSPLAAILAISL
GPWCCPC -> NSASSPASSGGGSTATHSSQ (in
isoform 5). {ECO:0000303|PubMed:1448111}.
/FTId=VSP_011276.
VAR_SEQ 590 599 Missing (in isoform 2).
{ECO:0000303|PubMed:1448111}.
/FTId=VSP_011273.
SEQUENCE 678 AA; 75740 MW; BB5C7DC1BD19E6BA CRC64;
MRPSQTALWL GLVLSLALLA VGWASARPPI YVSSWAVRVT KGYQEAERLA RKFGFVNLGQ
IFPDDQYFHL RHRGVAQQSL TPHWGHRLRL KKEPKVRWFE QQTLRRRVKR SLVVPTDPWF
SKQWYMNKEI EQDLNILKVW NQGLTGRGVV VSILDDGIEK DHPDLWANYD PLASYDFNDY
DPDPQPRYTP NDENRHGTRC AGEVSATANN GFCGAGVAFN ARIGGVRMLD GAITDIVEAQ
SLSLQPQHIH IYSASWGPED DGRTVDGPGL LTQEAFRRGV TKGRQGLGTL FIWASGNGGL
HYDNCNCDGY TNSIHTLSVG STTRQGRVPW YSEACASTFT TTFSSGVVTD PQIVTTDLHH
QCTDKHTGTS ASAPLAAGMI ALALEANPLL TWRDLQHLVV RASRPAQLQA EDWRINGVGR
QVSHHYGYGL LDAGLLVDLA RVWLPTKPQK KCTIRVVHTP TPILPRMLVP KNVTVCCDGS
RRRLIRSLEH VQVQLSLSYS RRGDLEIFLT SPMGTRSTLV AIRPLDISGQ GYNNWIFMST
HYWDEDPQGL WTLGLENKGY YYNTGTLYYC TLLLYGTAED MTARPQTPQE SHCPLSIVAE
LCLISSKQWW WLYSHTQQPV TKGQDSCHPP TTPARQLDQR LHCLFPAPHA GSASEPLQGL
SPLAAILAIS LGPWCCPC


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