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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: NEC1_MOUSE Q32MU0_MOUSE
LinkDB: NEC1_MOUSE Q32MU0_MOUSE
Original site: NEC1_MOUSE Q32MU0_MOUSE 
ID   NEC1_MOUSE              Reviewed;         753 AA.
AC   P63239; P21662; P22546;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   20-DEC-2017, entry version 124.
DE   RecName: Full=Neuroendocrine convertase 1;
DE            Short=NEC 1;
DE            EC=3.4.21.93;
DE   AltName: Full=Furin homolog;
DE   AltName: Full=PC3;
DE   AltName: Full=Prohormone convertase 1;
DE   AltName: Full=Propeptide-processing protease;
DE   AltName: Full=Proprotein convertase 1;
DE            Short=PC1;
DE   Flags: Precursor;
GN   Name=Pcsk1; Synonyms=Att-1, Nec-1, Nec1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=1862107; DOI=10.1073/pnas.88.15.6834;
RA   Korner J., Chun J., Harter D., Axel R.;
RT   "Isolation and functional expression of a mammalian prohormone
RT   processing enzyme, murine prohormone convertase 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6834-6838(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LAF1;
RX   PubMed=1657897;
RA   Nakayama K., Hosaka M., Hatsuzawa K., Murakami K.;
RT   "Cloning and functional expression of a novel endoprotease involved in
RT   prohormone processing at dibasic sites.";
RL   J. Biochem. 109:803-806(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Pituitary;
RX   PubMed=2017186; DOI=10.1210/mend-5-1-111;
RA   Seidah N.G., Marcinkiewicz M., Benjannet S., Gaspar L., Beaubien G.,
RA   Mattei M.-G., Lazure C., Mbikay M., Chretien M.;
RT   "Cloning and primary sequence of a mouse candidate prohormone
RT   convertase PC1 homologous to PC2, Furin, and Kex2: distinct
RT   chromosomal localization and messenger RNA distribution in brain and
RT   pituitary compared to PC2.";
RL   Mol. Endocrinol. 5:111-122(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 111-120.
RC   TISSUE=Ovary;
RX   PubMed=8449925;
RA   Zhou Y., Lindberg I.;
RT   "Purification and characterization of the prohormone convertase
RT   PC1(PC3).";
RL   J. Biol. Chem. 268:5615-5623(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 214-478.
RC   TISSUE=Pituitary;
RX   PubMed=2169760; DOI=10.1089/dna.1990.9.415;
RA   Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
RA   Chretien M.;
RT   "cDNA sequence of two distinct pituitary proteins homologous to Kex2
RT   and furin gene products: tissue-specific mRNAs encoding candidates for
RT   pro-hormone processing proteinases.";
RL   DNA Cell Biol. 9:415-424(1990).
RN   [6]
RP   ERRATUM.
RX   PubMed=2264933; DOI=10.1089/dna.1990.9.789;
RA   Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
RA   Chretien M.;
RL   DNA Cell Biol. 9:789-789(1990).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16384863; DOI=10.1210/en.2005-1373;
RA   Creemers J.W., Pritchard L.E., Gyte A., Le Rouzic P., Meulemans S.,
RA   Wardlaw S.L., Zhu X., Steiner D.F., Davies N., Armstrong D.,
RA   Lawrence C.B., Luckman S.M., Schmitz C.A., Davies R.A., Brennand J.C.,
RA   White A.;
RT   "Agouti-related protein is posttranslationally cleaved by proprotein
RT   convertase 1 to generate agouti-related protein (AGRP)83-132:
RT   interaction between AGRP83-132 and melanocortin receptors cannot be
RT   influenced by syndecan-3.";
RL   Endocrinology 147:1621-1631(2006).
RN   [8]
RP   STRUCTURE BY NMR OF 28-110.
RX   PubMed=12095256; DOI=10.1016/S0022-2836(02)00543-0;
RA   Tangrea M.A., Bryan P.N., Sari N., Orban J.;
RT   "Solution structure of the pro-hormone convertase 1 pro-domain from
RT   Mus musculus.";
RL   J. Mol. Biol. 320:801-812(2002).
CC   -!- FUNCTION: Involved in the processing of hormone and other protein
CC       precursors at sites comprised of pairs of basic amino acid
CC       residues. Substrates include POMC, renin, enkephalin, dynorphin,
CC       somatostatin, insulin and AGRP. {ECO:0000269|PubMed:16384863}.
CC   -!- CATALYTIC ACTIVITY: Release of protein hormones, neuropeptides and
CC       renin from their precursors, generally by hydrolysis of -Lys-
CC       Arg-|- bonds.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5-6.5.;
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-15770815, EBI-15770815;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC       Note=Localized in the secretion granules.
CC   -!- DISRUPTION PHENOTYPE: Increase in unprocessed AGRP.
CC       {ECO:0000269|PubMed:16384863}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
DR   EMBL; M69196; AAA39732.1; -; mRNA.
DR   EMBL; X57088; CAA40368.1; -; mRNA.
DR   EMBL; M58589; AAA39894.1; -; mRNA.
DR   EMBL; M55668; AAA39375.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS26649.1; -.
DR   PIR; JX0171; KXMSC1.
DR   RefSeq; NP_038656.1; NM_013628.2.
DR   RefSeq; XP_006517216.1; XM_006517153.2.
DR   RefSeq; XP_006517217.1; XM_006517154.3.
DR   RefSeq; XP_006517218.1; XM_006517155.2.
DR   UniGene; Mm.1333; -.
DR   UniGene; Mm.394672; -.
DR   PDB; 1KN6; NMR; -; A=28-110.
DR   PDB; 2KDT; NMR; -; A=711-753.
DR   PDB; 2KE3; NMR; -; A=711-753.
DR   PDBsum; 1KN6; -.
DR   PDBsum; 2KDT; -.
DR   PDBsum; 2KE3; -.
DR   ProteinModelPortal; P63239; -.
DR   SMR; P63239; -.
DR   DIP; DIP-48841N; -.
DR   STRING; 10090.ENSMUSP00000022075; -.
DR   MEROPS; S08.072; -.
DR   iPTMnet; P63239; -.
DR   PhosphoSitePlus; P63239; -.
DR   PaxDb; P63239; -.
DR   PeptideAtlas; P63239; -.
DR   PRIDE; P63239; -.
DR   Ensembl; ENSMUST00000022075; ENSMUSP00000022075; ENSMUSG00000021587.
DR   GeneID; 18548; -.
DR   KEGG; mmu:18548; -.
DR   UCSC; uc007rfs.1; mouse.
DR   CTD; 5122; -.
DR   MGI; MGI:97511; Pcsk1.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   GeneTree; ENSGT00750000117358; -.
DR   HOGENOM; HOG000192536; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; P63239; -.
DR   KO; K01359; -.
DR   OMA; FEPRALK; -.
DR   OrthoDB; EOG091G05HI; -.
DR   PhylomeDB; P63239; -.
DR   TreeFam; TF314277; -.
DR   BRENDA; 3.4.21.93; 3474.
DR   Reactome; R-MMU-209952; Peptide hormone biosynthesis.
DR   Reactome; R-MMU-264876; Insulin processing.
DR   Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   EvolutionaryTrace; P63239; -.
DR   PMAP-CutDB; P63239; -.
DR   PRO; PR:P63239; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000021587; -.
DR   CleanEx; MM_PCSK1; -.
DR   ExpressionAtlas; P63239; baseline and differential.
DR   Genevisible; P63239; MM.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
DR   GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR   CDD; cd04059; Peptidases_S8_Protein_converta; 1.
DR   Gene3D; 2.60.120.260; -; 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; IPR009020; Peptidase/Inhibitor_I9.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR022005; Proho_convert.
DR   InterPro; IPR032815; S8_pro-domain.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12177; Proho_convert; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   SUPFAM; SSF54897; SSF54897; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   PROPEP       28    110       {ECO:0000255}.
FT                                /FTId=PRO_0000027059.
FT   CHAIN       111    753       Neuroendocrine convertase 1.
FT                                /FTId=PRO_0000027060.
FT   DOMAIN      162    451       Peptidase S8.
FT   DOMAIN      460    597       P/Homo B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01173}.
FT   ACT_SITE    167    167       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    208    208       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    382    382       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    645    645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    225    374       {ECO:0000250}.
FT   DISULFID    317    347       {ECO:0000250}.
FT   DISULFID    467    494       {ECO:0000250}.
FT   CONFLICT    112    112       V -> F (in Ref. 2; CAA40368).
FT                                {ECO:0000305}.
FT   CONFLICT    117    117       A -> P (in Ref. 2; CAA40368).
FT                                {ECO:0000305}.
FT   CONFLICT    122    122       N -> T (in Ref. 2; CAA40368).
FT                                {ECO:0000305}.
FT   CONFLICT    128    128       Q -> H (in Ref. 2; CAA40368).
FT                                {ECO:0000305}.
FT   CONFLICT    282    282       R -> K (in Ref. 2; CAA40368).
FT                                {ECO:0000305}.
FT   CONFLICT    330    330       S -> L (in Ref. 3; AAA39375).
FT                                {ECO:0000305}.
FT   CONFLICT    732    732       K -> E (in Ref. 2; CAA40368).
FT                                {ECO:0000305}.
FT   STRAND       35     38       {ECO:0000244|PDB:1KN6}.
FT   HELIX        43     53       {ECO:0000244|PDB:1KN6}.
FT   STRAND       62     65       {ECO:0000244|PDB:1KN6}.
FT   STRAND       67     71       {ECO:0000244|PDB:1KN6}.
FT   STRAND       77     79       {ECO:0000244|PDB:1KN6}.
FT   HELIX        89     94       {ECO:0000244|PDB:1KN6}.
FT   STRAND       97    100       {ECO:0000244|PDB:1KN6}.
FT   STRAND      713    716       {ECO:0000244|PDB:2KDT}.
FT   STRAND      718    721       {ECO:0000244|PDB:2KE3}.
FT   HELIX       722    726       {ECO:0000244|PDB:2KDT}.
FT   TURN        727    730       {ECO:0000244|PDB:2KDT}.
FT   HELIX       741    748       {ECO:0000244|PDB:2KDT}.
FT   TURN        749    751       {ECO:0000244|PDB:2KDT}.
SQ   SEQUENCE   753 AA;  84174 MW;  04239C7B6385382E CRC64;
     MEQRGWTLQC TAFAFFCVWC ALNSVKAKRQ FVNEWAAEIP GGQEAASAIA EELGYDLLGQ
     IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE QQYEKERSKR SVQKDSALDL
     FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVITVLDDGL EWNHTDIYAN
     YDPEASYDFN DNDHDPFPRY DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
     LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
     SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
     TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
     ASNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECVVK DNNFEPRALK
     ANGEVIVEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE
     RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH
     MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN VEGRRDEQVQ
     GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF YEALEKLNKP SKLEGSEDSL
     YSDYVDVFYN TKPYKHRDDR LLQALMDILN EEN
//
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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (9)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (2)   
   ENSEMBL-UP (3)   
   MGI-MMU (1)   
Protein sequence (6)   
   RefSeq(pep) (4)   
   PMD (2)   
DNA sequence (4)   
   EMBL (4)   
3D Structure (3)   
   PDB (3)   
Protein domain (20)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (4)   
Literature (8)   
   PubMed (8)   
Enzyme (1)   
   BRENDA (1)   
All databases (62)   

Download RDF
ID   Q32MU0_MOUSE            Unreviewed;       753 AA.
AC   Q32MU0;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   20-DEC-2017, entry version 103.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 1 {ECO:0000313|EMBL:AAI08984.1};
GN   Name=Pcsk1 {ECO:0000313|EMBL:AAI08984.1, ECO:0000313|MGI:MGI:97511};
GN   ORFNames=mCG_15002 {ECO:0000313|EMBL:EDL37106.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI08984.1};
RN   [1] {ECO:0000313|EMBL:EDL37106.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL37106.1};
RX   PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [2] {ECO:0000313|EMBL:AAI08984.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI08984.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000313|EMBL:EDL37106.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL37106.1};
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.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS00679558}.
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DR   EMBL; BC108982; AAI08983.1; -; mRNA.
DR   EMBL; BC108983; AAI08984.1; -; mRNA.
DR   EMBL; CH466563; EDL37106.1; -; Genomic_DNA.
DR   RefSeq; NP_038656.1; NM_013628.2.
DR   RefSeq; XP_006517216.1; XM_006517153.2.
DR   RefSeq; XP_006517217.1; XM_006517154.3.
DR   RefSeq; XP_006517218.1; XM_006517155.2.
DR   UniGene; Mm.1333; -.
DR   UniGene; Mm.394672; -.
DR   GeneID; 18548; -.
DR   KEGG; mmu:18548; -.
DR   CTD; 5122; -.
DR   MGI; MGI:97511; Pcsk1.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   HOVERGEN; HBG008705; -.
DR   KO; K01359; -.
DR   OMA; FEPRALK; -.
DR   OrthoDB; EOG091G05HI; -.
DR   Bgee; ENSMUSG00000021587; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0043043; P:peptide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0016486; P:peptide hormone processing; IEA:Ensembl.
DR   CDD; cd04059; Peptidases_S8_Protein_converta; 1.
DR   Gene3D; 2.60.120.260; -; 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; IPR009020; Peptidase/Inhibitor_I9.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR022005; Proho_convert.
DR   InterPro; IPR032815; S8_pro-domain.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12177; Proho_convert; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   SUPFAM; SSF54897; SSF54897; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00912743};
KW   Protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00912730};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00912691}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    753       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011423395.
FT   DOMAIN      460    597       P/Homo B. {ECO:0000259|PROSITE:PS51829}.
SQ   SEQUENCE   753 AA;  84174 MW;  04239C7B6385382E CRC64;
     MEQRGWTLQC TAFAFFCVWC ALNSVKAKRQ FVNEWAAEIP GGQEAASAIA EELGYDLLGQ
     IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE QQYEKERSKR SVQKDSALDL
     FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVITVLDDGL EWNHTDIYAN
     YDPEASYDFN DNDHDPFPRY DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
     LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
     SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
     TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
     ASNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECVVK DNNFEPRALK
     ANGEVIVEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE
     RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH
     MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN VEGRRDEQVQ
     GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF YEALEKLNKP SKLEGSEDSL
     YSDYVDVFYN TKPYKHRDDR LLQALMDILN EEN
//
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Ontology (5)   
   GO (5)   
Gene (6)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (2)   
   MGI-MMU (1)   
Protein sequence (4)   
   RefSeq(pep) (4)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (20)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (4)   
Literature (2)   
   PubMed (2)   
All databases (40)   

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