ID   MCPT8_RAT               Reviewed;         248 AA.
AC   P97594;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2022, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Mast cell protease 8 {ECO:0000305};
DE            Short=rMCP-8;
DE            EC=3.4.21.-;
DE   AltName: Full=Mast cell protease VIII;
DE            Short=rMCP-VIII;
DE   Flags: Precursor;
GN   Name=Mcpt8 {ECO:0000312|RGD:3067};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=8996238; DOI=10.1084/jem.185.1.13;
RA   Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
RT   "Secretory granule proteases in rat mast cells. Cloning of 10 different
RT   serine proteases and a carboxypeptidase A from various rat mast cell
RT   populations.";
RL   J. Exp. Med. 185:13-29(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC       granules.
CC   -!- TISSUE SPECIFICITY: Mast cells.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; U67911; AAB48264.1; -; mRNA.
DR   EMBL; AABR07017922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_058842.1; NM_017146.1.
DR   RefSeq; NP_067609.1; NM_021598.2.
DR   RefSeq; XP_017455369.1; XM_017599880.1.
DR   AlphaFoldDB; P97594; -.
DR   SMR; P97594; -.
DR   STRING; 10116.ENSRNOP00000070668; -.
DR   MEROPS; S01.009; -.
DR   GlyCosmos; P97594; 3 sites, No reported glycans.
DR   GlyGen; P97594; 3 sites.
DR   PhosphoSitePlus; P97594; -.
DR   PaxDb; 10116-ENSRNOP00000027950; -.
DR   Ensembl; ENSRNOT00000099690.1; ENSRNOP00000097551.1; ENSRNOG00000063482.1.
DR   Ensembl; ENSRNOT00055020613; ENSRNOP00055016604; ENSRNOG00055012129.
DR   Ensembl; ENSRNOT00060042575; ENSRNOP00060035264; ENSRNOG00060024605.
DR   Ensembl; ENSRNOT00065054080; ENSRNOP00065044508; ENSRNOG00065031370.
DR   GeneID; 29269; -.
DR   GeneID; 54269; -.
DR   UCSC; RGD:3067; rat.
DR   AGR; RGD:3063; -.
DR   AGR; RGD:3067; -.
DR   CTD; 17231; -.
DR   CTD; 54269; -.
DR   RGD; 3067; Mcpt8.
DR   VEuPathDB; HostDB:ENSRNOG00000063482; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234551; -.
DR   InParanoid; P97594; -.
DR   OMA; PRIDPYN; -.
DR   OrthoDB; 4781966at2759; -.
DR   PhylomeDB; P97594; -.
DR   TreeFam; TF333630; -.
DR   PRO; PR:P97594; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000049991; Expressed in stomach and 13 other cell types or tissues.
DR   ExpressionAtlas; P97594; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   PANTHER; PTHR24271:SF22; MAST CELL PROTEASE 8; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P97594; RN.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..20
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027447"
FT   CHAIN           21..248
FT                   /note="Mast cell protease 8"
FT                   /id="PRO_0000027448"
FT   DOMAIN          21..243
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        108
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        37..49
FT                   /note="FIKFYDSNSEPHH -> SLMFYYGNSYRHY (in Ref. 1;
FT                   AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="R -> S (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="N -> K (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="S -> A (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103..105
FT                   /note="DSH -> HSR (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="V -> A (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..155
FT                   /note="RLANCTS -> CLANCSL (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="K -> E (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173..178
FT                   /note="QDMSED -> EDMSRN (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="V -> L (in Ref. 1; AAB48264)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   248 AA;  27463 MW;  6F362AFAE0E3D76F CRC64;
     MFLFLFFLVA ILPVNTEGGE IIWGTESKPH SRPYMAFIKF YDSNSEPHHC GGFLVAKDIV
     MTAAHCNGRN IKVTLGAHNI KKQENTQVIS VVKAKPHENY DRDSHFNDIM LLKLERKAQL
     NGVVKTIALP RSQDWVKPGQ VCTVAGWGRL ANCTSSNTLQ EVNLEVQKGQ KCQDMSEDYN
     DSIQLCVGNP SEGKATGKGD SGGPFVCDGV AQGIVSYRLC TGTLPRVFTR ISSFIPWIQK
     TMKVLQQS
//