ID A0A0R4J038_MOUSE Unreviewed; 661 AA. AC A0A0R4J038; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 28-MAR-2018, entry version 15. DE SubName: Full=Kininogen-1 {ECO:0000313|Ensembl:ENSMUSP00000023589}; GN Name=Kng1 {ECO:0000313|Ensembl:ENSMUSP00000023589, GN ECO:0000313|MGI:MGI:1097705}; 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|Ensembl:ENSMUSP00000023589, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000023589, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000023589, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000023589} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000023589}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00979}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC154540; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001095881.1; NM_001102411.1. DR UniGene; Mm.2160; -. DR SMR; A0A0R4J038; -. DR Ensembl; ENSMUST00000023589; ENSMUSP00000023589; ENSMUSG00000022875. DR GeneID; 16644; -. DR KEGG; mmu:16644; -. DR CTD; 3827; -. DR MGI; MGI:1097705; Kng1. DR GeneTree; ENSGT00440000039713; -. DR KO; K03898; -. DR OMA; GECTATV; -. DR Proteomes; UP000000589; Chromosome 16. DR ExpressionAtlas; A0A0R4J038; baseline and differential. DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-UniRule. DR CDD; cd00042; CY; 3. DR InterPro; IPR000010; Cystatin_dom. DR InterPro; IPR002395; Kininogen. DR InterPro; IPR027358; Kininogen-type_cystatin_dom. DR InterPro; IPR018073; Prot_inh_cystat_CS. DR Pfam; PF00031; Cystatin; 3. DR PRINTS; PR00334; KININOGEN. DR SMART; SM00043; CY; 3. DR PROSITE; PS00287; CYSTATIN; 1. DR PROSITE; PS51647; CYSTATIN_KININOGEN; 3. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00979}; KW Protease inhibitor {ECO:0000256|PROSITE-ProRule:PRU00979}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0R4J038, KW ECO:0000213|PeptideAtlas:A0A0R4J038}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Thiol protease inhibitor {ECO:0000256|PROSITE-ProRule:PRU00979}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 661 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006451928. FT DOMAIN 28 131 Cystatin kininogen-type. FT {ECO:0000259|PROSITE:PS51647}. FT DOMAIN 150 253 Cystatin kininogen-type. FT {ECO:0000259|PROSITE:PS51647}. FT DOMAIN 272 375 Cystatin kininogen-type. FT {ECO:0000259|PROSITE:PS51647}. FT DISULFID 83 96 {ECO:0000256|PROSITE-ProRule:PRU00979}. FT DISULFID 83 94 {ECO:0000256|PROSITE-ProRule:PRU00979}. FT DISULFID 228 247 {ECO:0000256|PROSITE-ProRule:PRU00979}. FT DISULFID 350 369 {ECO:0000256|PROSITE-ProRule:PRU00979}. SQ SEQUENCE 661 AA; 73101 MW; 7744602F8DF8796E CRC64; MKLITTLLLC SGLLLTLTQG EEAQEIDCND EAVFQAVDFS LKQFNPGVKS GNQYMLHRVI EGTKTDGSPT FYSFKYLIKE GNCSAQSGLA WQDCDFKDAE EAATGECTAT VGKRENEFFI VTQTCKIAPS KAPILKAYFP CIGCVHAIST DSPDLEPVLK HSIEHFNNNT DHSHLFTLRK VKSAHRQVVA GLNFDITYTI VQTNCSKERF PSLHGDCVAL PNGDDGECRG NLFMDINNKI ANFSQSCTLY SGDDLVEALP KPCPGCPRDI PVDSPELKEV LGHSIAQLNA ENDHPFYYKI DTVKKATSQV VAGTKYVIEF IARETKCSKE SNTELAEDCE IKHLGQSLDC NANVYMRPWE NKVVPTVKCQ ALDMTEMARR PPGFSPFRSV TVQETKEGRT VSPPYIAREQ EERDAETEQG PTHGHGWLHE KQIKANKNHR GHKHGHDHGH WSPRRHGLGH GHQKPHGLGH GHQLKLDYLR HQREDGDDHT HTVGHGHGHG HGHGHGHGHG HGHGHGHGHG HGHGKHTNKD KNSVKQTTQR TESLASSSEY STTSTQMQGR TEGPTLTPPR AQPTVTSSGF QDSDFIEDVV ATTPPYDTGA HDDLIPDIHV QPDSLSFKLI SDFPEATSPK CPGRPWKPAS WKDPNTETTE FSDFDLLDAL S //