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Database: UniProt/TrEMBL
Entry: A0A1W2VS61_CIOIN A1IHD0_CIOIN
LinkDB: A0A1W2VS61_CIOIN A1IHD0_CIOIN
Original site: A0A1W2VS61_CIOIN A1IHD0_CIOIN 
ID   A0A1W2VS61_CIOIN        Unreviewed;       660 AA.
AC   A0A1W2VS61;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   30-AUG-2017, entry version 3.
DE   SubName: Full=Neuroendocrine convertase 2-like {ECO:0000313|RefSeq:NP_001128498.1};
DE            EC=3.4.21.94 {ECO:0000313|RefSeq:NP_001128498.1};
GN   Name=cipc2 {ECO:0000313|RefSeq:NP_001128498.1};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona;
OC   Phlebobranchia; Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|Proteomes:UP000192222, ECO:0000313|RefSeq:NP_001128498.1};
RN   [1] {ECO:0000313|RefSeq:NP_001128498.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17070810; DOI=10.1016/j.ygcen.2006.08.010;
RA   Sekiguchi T., Kawashima T., Satou Y., Satoh N.;
RT   "Further EST analysis of endocrine genes that are preferentially
RT   expressed in the neural complex of Ciona intestinalis: receptor and
RT   enzyme genes associated with endocrine system in the neural complex.";
RL   Gen. Comp. Endocrinol. 150:233-245(2007).
RN   [2] {ECO:0000313|RefSeq:NP_001128498.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JUN-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS00679558}.
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DR   RefSeq; NP_001128498.1; NM_001135026.1.
DR   GeneID; 100181292; -.
DR   Proteomes; UP000192222; Genome assembly.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 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   Complete proteome {ECO:0000313|Proteomes:UP000192222};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00066207};
KW   Protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00066236};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00066164}.
FT   DOMAIN       54    134       S8_pro-domain. {ECO:0000259|Pfam:
FT                                PF16470}.
FT   DOMAIN      183    470       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
FT   DOMAIN      529    615       P_proprotein. {ECO:0000259|Pfam:PF01483}.
SQ   SEQUENCE   660 AA;  72590 MW;  D03A15473DB6E005 CRC64;
     MADNCYAGQT RSFSRALSYI LLLTLMSWDT DLAGIRTGSL LVSAAKKRVY TNDFLVTIKS
     AEPSSNHDHA DWLAARHGFE NRGMVVGDEG LYHFRHRTLD SASESPSLRY IWNLRLSPKV
     QKVRQLEGYG RLKRGHNKVK VGAYQGLDPL YPYQWYINNT GQAGGKPGLD LNVQAAWNMG
     YTGKGVTVAI MDDGLDYLHP DLRDNYSPEA SYDFSSNDPY PYPRYTFNWF NSHGTRCAGE
     VSSVADNGIC GVGVAYDSKI AGIRMLDQPF MTDVIEAASM SFKPNLIDIY SASWGPTDDG
     KTVDGPRQLT LRAIVNGVNK GRNGLGSIYV WASGDGGADD DCNCDGYAAS MWTISVNSAI
     NDGETALYDE SCSSTLASTF SNGRGQRAGS GVATTDLYGQ CTLRHSGTSA AAPEAAGVFA
     LALDANKNLT WRDVQHLTVL TSTPNLLHDD LHRWQSNGVG LMFNHLFGFG VLNAQKMVKM
     AKTWTTVPPR FRCEAGVVEQ MFDIPSDGVL ELTIDTDACD GGNNHVRYLE HVQAFLTIAS
     SRRGDLTINM TSPFGTDSIL LNRRPNDDDS SQGFRKWPFM TTHTWGEDPR GTWKLRVALN
     GEFPQTGRLL RWGLLLHGTQ QAPYIDEILD GHNSKLAVSK KLEFAEGILH DLEDSGSQHP
//
  All links  
Ontology (1)   
   GO (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (3)   
Literature (1)   
   PubMed (1)   
All databases (22)   

Download RDF
ID   A1IHD0_CIOIN            Unreviewed;       660 AA.
AC   A1IHD0;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   05-JUL-2017, entry version 60.
DE   SubName: Full=Putative prohormone convertase 2 {ECO:0000313|EMBL:BAF42696.1};
DE            EC=3.4.21.94 {ECO:0000313|EMBL:BAF42696.1};
GN   Name=CiPC2 {ECO:0000313|EMBL:BAF42696.1};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona;
OC   Phlebobranchia; Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|EMBL:BAF42696.1};
RN   [1] {ECO:0000313|EMBL:BAF42696.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17070810; DOI=10.1016/j.ygcen.2006.08.010;
RA   Sekiguchi T., Kawashima T., Satou Y., Satoh N.;
RT   "Further EST analysis of endocrine genes that are preferentially
RT   expressed in the neural complex of Ciona intestinalis: receptor and
RT   enzyme genes associated with endocrine system in the neural complex.";
RL   Gen. Comp. Endocrinol. 150:233-245(2007).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS00679558}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB250763; BAF42696.1; -; mRNA.
DR   RefSeq; NP_001128498.1; NM_001135026.1.
DR   UniGene; Cin.32722; -.
DR   ProteinModelPortal; A1IHD0; -.
DR   MEROPS; S08.073; -.
DR   GeneID; 100181292; -.
DR   KEGG; cin:100181292; -.
DR   CTD; 100181292; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; KOG3526; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   HOVERGEN; HBG008705; -.
DR   KO; K01360; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 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   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00066207, ECO:0000313|EMBL:BAF42696.1};
KW   Protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00066236};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS00066164}.
FT   DOMAIN       54    134       S8_pro-domain. {ECO:0000259|Pfam:
FT                                PF16470}.
FT   DOMAIN      183    470       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
FT   DOMAIN      529    615       P_proprotein. {ECO:0000259|Pfam:PF01483}.
SQ   SEQUENCE   660 AA;  72590 MW;  D03A15473DB6E005 CRC64;
     MADNCYAGQT RSFSRALSYI LLLTLMSWDT DLAGIRTGSL LVSAAKKRVY TNDFLVTIKS
     AEPSSNHDHA DWLAARHGFE NRGMVVGDEG LYHFRHRTLD SASESPSLRY IWNLRLSPKV
     QKVRQLEGYG RLKRGHNKVK VGAYQGLDPL YPYQWYINNT GQAGGKPGLD LNVQAAWNMG
     YTGKGVTVAI MDDGLDYLHP DLRDNYSPEA SYDFSSNDPY PYPRYTFNWF NSHGTRCAGE
     VSSVADNGIC GVGVAYDSKI AGIRMLDQPF MTDVIEAASM SFKPNLIDIY SASWGPTDDG
     KTVDGPRQLT LRAIVNGVNK GRNGLGSIYV WASGDGGADD DCNCDGYAAS MWTISVNSAI
     NDGETALYDE SCSSTLASTF SNGRGQRAGS GVATTDLYGQ CTLRHSGTSA AAPEAAGVFA
     LALDANKNLT WRDVQHLTVL TSTPNLLHDD LHRWQSNGVG LMFNHLFGFG VLNAQKMVKM
     AKTWTTVPPR FRCEAGVVEQ MFDIPSDGVL ELTIDTDACD GGNNHVRYLE HVQAFLTIAS
     SRRGDLTINM TSPFGTDSIL LNRRPNDDDS SQGFRKWPFM TTHTWGEDPR GTWKLRVALN
     GEFPQTGRLL RWGLLLHGTQ QAPYIDEILD GHNSKLAVSK KLEFAEGILH DLEDSGSQHP
//
  All links  
Ontology (1)   
   GO (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (3)   
Literature (1)   
   PubMed (1)   
All databases (25)   

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