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IPSG_VULVU
ID   IPSG_VULVU              Reviewed;         115 AA.
AC   P08479;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Double-headed protease inhibitor, submandibular gland;
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Submandibular gland;
RX   PubMed=3393515;
RA   Reisinger P.W.M., Hochstrasser K., Wachter E.;
RT   "The amino-acid sequence of the double-headed proteinase inhibitor from fox
RT   (Vulpes vulpes) submandibular glands.";
RL   Protein Seq. Data Anal. 1:259-261(1988).
CC   -!- FUNCTION: This inhibitor is composed of two homologous actively
CC       inhibiting halves: one which inhibits trypsin, the other which inhibits
CC       elastase.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   PIR; S03371; S03371.
DR   AlphaFoldDB; P08479; -.
DR   SMR; P08479; -.
DR   MEROPS; I01.016; -.
DR   MEROPS; I01.017; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001239; Prot_inh_Kazal-m.
DR   Pfam; PF00050; Kazal_1; 2.
DR   PRINTS; PR00290; KAZALINHBTR.
DR   SMART; SM00280; KAZAL; 2.
DR   SUPFAM; SSF100895; SSF100895; 2.
DR   PROSITE; PS00282; KAZAL_1; 2.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Repeat; Secreted; Serine protease inhibitor.
FT   CHAIN           1..115
FT                   /note="Double-headed protease inhibitor, submandibular
FT                   gland"
FT                   /id="PRO_0000073042"
FT   DOMAIN          6..66
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          67..115
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            26..27
FT                   /note="Reactive bond 1 for trypsin"
FT   SITE            77..78
FT                   /note="Reactive bond 2 for elastase"
FT   DISULFID        12..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        32..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        68..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        75..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        83..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   115 AA;  12818 MW;  104660EC41AC397F CRC64;
     DPPPAIGREV DCSSYKGKGS QIACPRHLQP ICGTDHNTYS NECMFCALTL NKEFEVRKLQ
     DTACDIECTE YSDMCTMDYR PLCGSDGKNY SNKCIFCNAV VRSRGTIFLA KHGEC
 
 
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