GenomeNet

Database: UniProt/TrEMBL
Entry: F1PKR4_CANLF
LinkDB: F1PKR4_CANLF
Original site: F1PKR4_CANLF 
ID   F1PKR4_CANLF            Unreviewed;       638 AA.
AC   F1PKR4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   25-OCT-2017, entry version 44.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 2 {ECO:0000313|Ensembl:ENSCAFP00000008234};
GN   Name=PCSK2 {ECO:0000313|Ensembl:ENSCAFP00000008234};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000008234, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000008234, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000008234,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000008234}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000008234};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS00679558}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000008234}.
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DR   EMBL; AAEX03013773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03013774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003433232.1; XM_003433184.3.
DR   ProteinModelPortal; F1PKR4; -.
DR   STRING; 9615.ENSCAFP00000008234; -.
DR   MEROPS; S08.073; -.
DR   PaxDb; F1PKR4; -.
DR   Ensembl; ENSCAFT00000008876; ENSCAFP00000008234; ENSCAFG00000005498.
DR   GeneID; 485757; -.
DR   KEGG; cfa:485757; -.
DR   CTD; 5126; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; KOG3526; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   GeneTree; ENSGT00750000117358; -.
DR   InParanoid; F1PKR4; -.
DR   KO; K01360; -.
DR   OMA; PQRGVLK; -.
DR   OrthoDB; EOG091G05HI; -.
DR   TreeFam; TF314277; -.
DR   Proteomes; UP000002254; Chromosome 24.
DR   Bgee; ENSCAFG00000005498; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0034230; P:enkephalin processing; IEA:Ensembl.
DR   GO; GO:0030070; P:insulin processing; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR   GO; GO:0016540; P:protein autoprocessing; 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.
DR   InterPro; IPR034182; Kexin/furin.
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; IPR002884; PrprotnconvertsP.
DR   InterPro; IPR032815; S8_pro-domain.
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   SUPFAM; SSF54897; SSF54897; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00912743};
KW   Protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00912730};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00912691}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    638       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003267440.
FT   DOMAIN       33    109       S8_pro-domain. {ECO:0000259|Pfam:
FT                                PF16470}.
FT   DOMAIN      158    420       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
FT   DOMAIN      504    590       P_proprotein. {ECO:0000259|Pfam:PF01483}.
FT   COILED      609    636       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   638 AA;  70606 MW;  27F81A55E9A51318 CRC64;
     MKGGRVSQWK AAAGLLFCVM VFASAERPVL TNHFLVELHQ GGEEEARQVA AEHGFGVRKL
     PFTEGLYHFY HNGLAKAKRR RSLHHKQQLE RDPRVKMALQ QEGFNRKKRG YRDINEIDIN
     MNDPLFTKQW YLINTGQADG TPGLDLNVAE AWELGYTGKG VTIGIMDDGI DYLHPDLASN
     YNAEASYDFS GNDPYPYPRY TDDWFNSHGT RCAGEVSAAA NNNICGVGVA YNSKVAGIRM
     LDQPFMTDII EASSISHMPQ LIDIYSASWG PTDNGKTVDG PRELTLQAMA DGVNKGRGGK
     GSIYVWASGD GGSYDDCNCD GYASSMWTIS INSAINDGRT ALYDESCSST LASTFSNGRK
     RNPEAGVATT DLYGNCTLRH SGTSAAAPEA AGVFALALEA NLGLTWRDMQ HLTVLTSKRN
     QLHDEVHQWR RNGVGLEFNH LFGYGVLDAG AMVKMAKDWK TVPERFHCVG GSVQDPEKIP
     STGKLVLTLT TDACEGKENF VRYLEHVQAV ITVNATRRGD LNINMTSPMG TKSILLSRRP
     RDDDSKVGFD KWPFMTTHTW GEDARGTWTL ELGFVGSAPQ KGVLKEWTLM LHGTQSAPYI
     DQVVRDYQSK LAMSKKEELE EELDEAVERS LKSILRKN
//
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