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KNG_SALSA
ID   KNG_SALSA               Reviewed;         375 AA.
AC   A0A1S3PBB7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Kininogen;
DE   Contains:
DE     RecName: Full=Bradykinin;
DE   Flags: Precursor;
GN   Name=LOC106584303;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle;
RA   Lien S., Koop B.F., Miller J.R., Kent M.P., Sandve S.R., Nome T.,
RA   Hvidsten T.R., Grammes F., Grove H., Gjuvsland A., Karloss J., Vage D.I.,
RA   Leong J.S., Minkley D., von Schalburg K., Rondeau E., Zimin A., Walenz B.,
RA   Di Genova A., Smith D., Grimholt U., de Jong P., Moen T., Maass A.,
RA   Vidal R., Iturra P., Jones S.J.M., Jonassen I., Omholt S.W., Davidson W.S.;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, FUNCTION, MASS
RP   SPECTROMETRY, AND GLYCOSYLATION.
RX   PubMed=10583403; DOI=10.1046/j.1432-1327.1999.00950.x;
RA   Yloenen A., Rinne A., Herttuainen J., Bogwald J., Jaervinen M.,
RA   Kalkkinen N.;
RT   "Atlantic salmon (Salmo salar L.) skin contains a novel kininogen and
RT   another cysteine proteinase inhibitor.";
RL   Eur. J. Biochem. 266:1066-1072(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 72-87 AND 218-244, AND GLYCOSYLATION AT ASN-74 AND
RP   ASN-235.
RX   PubMed=11447131; DOI=10.1093/glycob/11.7.523;
RA   Yloenen A., Kalkkinen N., Saarinen J., Boegwald J., Helin J.;
RT   "Glycosylation analysis of two cysteine proteinase inhibitors from Atlantic
RT   salmon skin: di-O-acetylated sialic acids are the major sialic acid species
RT   on N-glycans.";
RL   Glycobiology 11:523-531(2001).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12397376; DOI=10.1007/s00441-002-0627-7;
RA   Taehtinen V., Weber E., Guenther D., Yloenen A., Kalkkinen N., Olsen R.,
RA   Jaervinen M., Soederstroem K.O., Rinne A., Bjoerklund H., Boegwald J.;
RT   "Immunolocalization of cysteine proteinases (cathepsins) and cysteine
RT   proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon,
RT   Salmo salar.";
RL   Cell Tissue Res. 310:213-222(2002).
CC   -!- FUNCTION: Inhibits papain and ficin (cysteine proteinases) but not
CC       trypsin (a serine proteinase). {ECO:0000269|PubMed:10583403}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12397376}. Vacuole
CC       {ECO:0000269|PubMed:12397376}.
CC   -!- TISSUE SPECIFICITY: Expressed in the skin, liver, intestine, spleen,
CC       pancreas and kidney. {ECO:0000269|PubMed:12397376}.
CC   -!- PTM: N-glycosylated, with sialylated biantennary complex-type glycans.
CC       {ECO:0000269|PubMed:11447131}.
CC   -!- PTM: O-glycosylated, sialylated oligosaccharides.
CC       {ECO:0000269|PubMed:11447131}.
CC   -!- PTM: Bradykinin is released from kininogen by kallikrein.
CC       {ECO:0000250|UniProtKB:P01042}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10583403}.
CC   -!- MASS SPECTROMETRY: [Kininogen]: Mass=52000; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10583403};
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DR   EMBL; AGKD04000030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_014024862.1; XM_014169387.1.
DR   STRING; 8030.ENSSSAP00000084884; -.
DR   GeneID; 106584303; -.
DR   KEGG; sasa:106584303; -.
DR   OMA; VAERTMC; -.
DR   OrthoDB; 740995at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa23.
DR   Bgee; ENSSSAG00000068757; Expressed in liver and 7 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005773; C:vacuole; IDA:UniProtKB.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   CDD; cd00042; CY; 2.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR027358; Kininogen-type_cystatin_dom.
DR   Pfam; PF00031; Cystatin; 2.
DR   SMART; SM00043; CY; 2.
DR   SUPFAM; SSF54403; SSF54403; 2.
DR   PROSITE; PS51647; CYSTATIN_KININOGEN; 2.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Signal; Thiol protease inhibitor; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:10583403"
FT   CHAIN           24..375
FT                   /note="Kininogen"
FT                   /id="PRO_5010208301"
FT   PEPTIDE         268..276
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:P01042"
FT                   /id="PRO_0000455009"
FT   DOMAIN          35..139
FT                   /note="Cystatin kininogen-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT   DOMAIN          156..260
FT                   /note="Cystatin kininogen-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT   REGION          283..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11447131"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11447131"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT   DISULFID        115..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT   DISULFID        211..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
FT   DISULFID        234..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00979"
SQ   SEQUENCE   375 AA;  41560 MW;  8027FD71627713AA CRC64;
     MKLGVRLCVL VVFSLQLWGP GQGQELEPEQ VLAFCDDKDV EAAVDLALVK YNQKLPYGNQ
     LALYQILESS KAQNDSCTQY FVEFNSRVTD CPAGGDKVWR DCDYLPTGNK VPRPCKATVH
     MSETDKKVLA VFCDPVEAPV VAERTTCLGC PREIDVESED LKDPLTYSIT RFNADSDSSH
     HFILNSVGFA TRQVVAGFRY RLMFDMRKSN CSKADHKELN DECHPDPDVE LAHCNSTVDV
     APWRHETAEA NVECAPGPLD NFDVFRRRPP GWSPLRNFNN FAEVKTTQAS TASAKEESSE
     ESQERSPSAV TMANPEPALP SVAPTTAAES PFHCPSKPWK QFVPPTTLRP AQEKSPTPLP
     VVEEGLSDLD LLGKK
 
 
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