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CAP7_PIG
ID   CAP7_PIG                Reviewed;         246 AA.
AC   P80015;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Azurocidin {ECO:0000250|UniProtKB:P20160};
DE   AltName: Full=Cationic antimicrobial protein CAP37 {ECO:0000250|UniProtKB:P20160};
DE   AltName: Full=Heparin-binding protein {ECO:0000303|PubMed:2026172};
DE            Short=HBP {ECO:0000303|PubMed:2026172};
DE            Short=pHBP {ECO:0000303|PubMed:2026172};
DE   Flags: Precursor;
GN   Name=AZU1 {ECO:0000250|UniProtKB:P20160};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 27-245, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   FUNCTION.
RC   TISSUE=Neutrophil;
RX   PubMed=2026172; DOI=10.1111/j.1432-1033.1991.tb15942.x;
RA   Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J., Engels M.,
RA   Wollmer A.;
RT   "Covalent structure of two novel neutrophile leucocyte-derived proteins of
RT   porcine and human origin. Neutrophile elastase homologues with strong
RT   monocyte and fibroblast chemotactic activities.";
RL   Eur. J. Biochem. 197:535-547(1991).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-139 AND
RP   ASN-170, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=2076469; DOI=10.1002/bms.1200191110;
RA   Sorensen H.H., Thomsen J., Bayne S., Hojrup P., Roepstorff P.;
RT   "Strategies for determination of disulphide bridges in proteins using
RT   plasma desorption mass spectrometry.";
RL   Biomed. Environ. Mass Spectrom. 19:713-720(1990).
CC   -!- FUNCTION: This is a neutrophil granule-derived antibacterial and
CC       monocyte- and fibroblast-specific chemotactic glycoprotein. Binds
CC       heparin. {ECO:0000250|UniProtKB:P20160, ECO:0000269|PubMed:2026172}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
CC       {ECO:0000250|UniProtKB:P20160}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P20160}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P20160}. Note=Localizes to azurophil granules of
CC       neutrophil granulocytes. Also called primary granules, these
CC       specialized lysosomes of the neutrophil formed early during
CC       promyelocyte development store antibacterial proteins and peptides.
CC       {ECO:0000250|UniProtKB:P20160}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; JH115037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S15393; TRPGAZ.
DR   RefSeq; XP_005661477.1; XM_005661420.2.
DR   AlphaFoldDB; P80015; -.
DR   SMR; P80015; -.
DR   STRING; 9823.ENSSSCP00000014264; -.
DR   MEROPS; S01.971; -.
DR   iPTMnet; P80015; -.
DR   PaxDb; P80015; -.
DR   PeptideAtlas; P80015; -.
DR   PRIDE; P80015; -.
DR   Ensembl; ENSSSCT00000014659; ENSSSCP00000014264; ENSSSCG00000013415.
DR   Ensembl; ENSSSCT00005029743; ENSSSCP00005018106; ENSSSCG00005018835.
DR   Ensembl; ENSSSCT00015081055; ENSSSCP00015032789; ENSSSCG00015060634.
DR   Ensembl; ENSSSCT00025010233; ENSSSCP00025004099; ENSSSCG00025007701.
DR   Ensembl; ENSSSCT00030023951; ENSSSCP00030010745; ENSSSCG00030017322.
DR   Ensembl; ENSSSCT00035100473; ENSSSCP00035042669; ENSSSCG00035074066.
DR   Ensembl; ENSSSCT00040088326; ENSSSCP00040038828; ENSSSCG00040064681.
DR   Ensembl; ENSSSCT00045052007; ENSSSCP00045036193; ENSSSCG00045030459.
DR   Ensembl; ENSSSCT00055047471; ENSSSCP00055037890; ENSSSCG00055024074.
DR   Ensembl; ENSSSCT00065009896; ENSSSCP00065004119; ENSSSCG00065007386.
DR   Ensembl; ENSSSCT00070053760; ENSSSCP00070045580; ENSSSCG00070026803.
DR   GeneID; 100522363; -.
DR   KEGG; ssc:100522363; -.
DR   CTD; 566; -.
DR   VGNC; VGNC:85714; AZU1.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234551; -.
DR   HOGENOM; CLU_006842_1_0_1; -.
DR   InParanoid; P80015; -.
DR   OMA; TAYRSWI; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF335284; -.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Proteomes; UP000314985; Chromosome 2.
DR   Bgee; ENSSSCG00000013415; Expressed in blood and 8 other tissues.
DR   ExpressionAtlas; P80015; differential.
DR   Genevisible; P80015; SS.
DR   GO; GO:0042582; C:azurophil granule; ISS:UniProtKB.
DR   GO; GO:0035577; C:azurophil granule membrane; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0019730; P:antimicrobial humoral response; IEA:Ensembl.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
DR   GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0008347; P:glial cell migration; ISS:UniProtKB.
DR   GO; GO:0001774; P:microglial cell activation; ISS:UniProtKB.
DR   GO; GO:0070944; P:neutrophil-mediated killing of bacterium; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0032724; P:positive regulation of fractalkine production; ISS:UniProtKB.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR   GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Chemotaxis; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Heparin-binding; Membrane;
KW   Reference proteome; Serine protease homolog; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:P20160"
FT   PROPEP          20..26
FT                   /evidence="ECO:0000305|PubMed:2026172"
FT                   /id="PRO_0000435374"
FT   CHAIN           27..245
FT                   /note="Azurocidin"
FT                   /evidence="ECO:0000269|PubMed:2026172"
FT                   /id="PRO_0000088679"
FT   PROPEP          245..246
FT                   /evidence="ECO:0000269|PubMed:2026172"
FT                   /id="PRO_0000435375"
FT   DOMAIN          27..242
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2076469"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2076469"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000269|PubMed:2076469"
FT   DISULFID        148..205
FT                   /evidence="ECO:0000269|PubMed:2076469"
FT   DISULFID        178..184
FT                   /evidence="ECO:0000269|PubMed:2076469"
SQ   SEQUENCE   246 AA;  27039 MW;  E0731B1E2BA4A447 CRC64;
     MPALRFLALL ASLLATSRVG LATLADIVGG RRAQPQEFPF LASIQKQGRP FCAGALVHPR
     FVLTAASCFR GKNSGSASVV LGAYDLRQQE QSRQTFSIRS ISQNGYDPRQ NLNDVLLLQL
     DREARLTPSV ALVPLPPQNA TVEAGTNCQV AGWGTQRLRR LFSRFPRVLN VTVTSNPCLP
     RDMCIGVFSR RGRISQGDRG TPLVCNGLAQ GVASFLRRRF RRSSGFFTRV ALFRNWIDSV
     LNNPPA
 
 
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