ID   SALRN_SALAL             Reviewed;         342 AA.
AC   Q70SU7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Cystein proteinase inhibitor protein salarin;
DE   Flags: Precursor;
GN   Name=salarin;
OS   Salvelinus alpinus (Arctic char) (Salmo alpinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salvelinus.
OX   NCBI_TaxID=8036 {ECO:0000312|EMBL:CAD80247.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN
RP   SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=14505823; DOI=10.1016/s0300-9084(03)00128-7;
RA   Olonen A., Kalkkinen N., Paulin L.;
RT   "A new type of cysteine proteinase inhibitor--the salarin gene from
RT   Atlantic salmon (Salmo salar L.) and Arctic charr (Salvelinus alpinus).";
RL   Biochimie 85:677-681(2003).
CC   -!- FUNCTION: Inhibits papain and ficin (cysteine proteinases) but not
CC       trypsin (a serine proteinase). {ECO:0000250|UniProtKB:Q70SU8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q70SU8}. Vacuole
CC       {ECO:0000250|UniProtKB:Q70SU8}.
CC   -!- PTM: N-glycosylated, with sialylated biantennary complex-type glycans.
CC       {ECO:0000250|UniProtKB:Q70SU8}.
CC   -!- PTM: O-glycosylated, with sialylated oligosaccharides.
CC       {ECO:0000250|UniProtKB:Q70SU8}.
CC   -!- MASS SPECTROMETRY: [Cystein proteinase inhibitor protein salarin]:
CC       Mass=43000; Method=MALDI; Evidence={ECO:0000269|PubMed:14505823};
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DR   EMBL; AJ550229; CAD80247.1; -; mRNA.
DR   MEROPS; I29.951; -.
DR   OrthoDB; 913450at2759; -.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 4.
DR   SMART; SM00848; Inhibitor_I29; 4.
DR   SUPFAM; SSF54001; SSF54001; 4.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW   Signal; Thiol protease inhibitor; Vacuole.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:14505823"
FT   CHAIN           20..342
FT                   /note="Cystein proteinase inhibitor protein salarin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004283505"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q70SU8"
FT   CARBOHYD        184
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q70SU8"
SQ   SEQUENCE   342 AA;  39689 MW;  D69CC96840C7046E CRC64;
     MKSLVLLLLV AVTVSSVVSK PLPEDSEAEV HKEFETWKVK YGKSYPSTEE EAKRKEMWLA
     TRKRVMEHNT RAGNGLESYT MAVNHFADLT TEEVPKGLLP MPRPEEEEVD KEFEMWKTVN
     GKTYNSTEEE ARRKEIWLAT RARVMEHNKR AENGSESFTM GINYFSDMTF EEVPKGRLMV
     VFPTRDGGEE AEVDKEFEMW KVQHGKSYGS TEEEAKRKEI WLATRTRVME HNKRAETGLE
     SFTMGMNHLS DKTTAEVTGQ RLQDREEAEV HKEFETWKVK YGKTYPSTEE EAKRKEIWLA
     TRKMVTEHNK RAENGQESFT MAVNHFADLT TEEVPKGLLP ME