SALRN_SALSA
ID SALRN_SALSA Reviewed; 342 AA.
AC Q70SU8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cystein proteinase inhibitor protein salarin;
DE AltName: Full=Cathepsin M;
DE Flags: Precursor;
GN Name=salarin; Synonyms=catm;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL
RP PROTEIN 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Head kidney;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 151-175 AND 178-201, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND GLYCOSYLATION AT ASN-153 AND THR-184.
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 [5]
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, with sialylated oligosaccharides.
CC {ECO:0000269|PubMed:11447131}.
CC -!- MASS SPECTROMETRY: [Cystein proteinase inhibitor protein salarin]:
CC Mass=43000; Method=MALDI; Evidence={ECO:0000269|PubMed:10583403,
CC ECO:0000269|PubMed:14505823};
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DR EMBL; AJ550228; CAD80246.1; -; Genomic_DNA.
DR EMBL; BT046998; ACI66799.1; -; mRNA.
DR RefSeq; NP_001134251.1; NM_001140779.1.
DR SMR; Q70SU8; -.
DR MEROPS; I29.951; -.
DR GeneID; 100195750; -.
DR KEGG; sasa:100195750; -.
DR OrthoDB; 913450at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR Bgee; ENSSSAG00000080729; Expressed in liver and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005773; C:vacuole; IDA:AgBase.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:AgBase.
DR GO; GO:0002020; F:protease binding; IDA:AgBase.
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 Reference proteome; 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_5009732209"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:11447131"
FT CARBOHYD 184
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:11447131"
SQ SEQUENCE 342 AA; 39496 MW; 95568CA862837EA0 CRC64;
MKSLVLLLLV AVTVSSVVSK PLPEDSEAEV HKEFETWKVK YGKSYPSTEE EAKRKEMWLA
TRKKVMEHNT RAGNGLESYT MAVNHLADLT TEEVPKGLLP MPRPEEEEVD KEFEMWKTHN
GKTYNSTEEE AKRKEIWLAT RARVMEHNKR AENGSESFTM GINYFSDMTF EEIPKARLMV
VFPTRDGGEE AEVDKEFETW KVQHGKNYGS TEEEAKRKGI WLATRTRVME HNKRAETGSE
SFTMGMNHLS DKTTAEVTGR RLQDGEEAEV HKEFETWKVK YGKTYPSTVE EAKRKEIWLA
TRKMVMEHNK RAENGLESFT MGVNHFADLT AEEVPRGLFP ME
