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Database: UniProt
Entry: D3ZQJ8_RAT
LinkDB: D3ZQJ8_RAT
Original site: D3ZQJ8_RAT 
ID   D3ZQJ8_RAT              Unreviewed;       607 AA.
AC   D3ZQJ8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Serine protease 56 {ECO:0000313|Ensembl:ENSRNOP00000060294.2};
GN   Name=Prss56 {ECO:0000313|Ensembl:ENSRNOP00000060294.2,
GN   ECO:0000313|RGD:1563955};
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 {ECO:0000313|Ensembl:ENSRNOP00000060294.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000060294.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060294.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000060294.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060294.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_003750778.1; XM_003750730.4.
DR   RefSeq; XP_003754590.1; XM_003754542.4.
DR   AlphaFoldDB; D3ZQJ8; -.
DR   SMR; D3ZQJ8; -.
DR   STRING; 10116.ENSRNOP00000060294; -.
DR   MEROPS; S01.514; -.
DR   PaxDb; 10116-ENSRNOP00000060294; -.
DR   Ensembl; ENSRNOT00000065805.3; ENSRNOP00000060294.2; ENSRNOG00000029865.5.
DR   GeneID; 363274; -.
DR   KEGG; rno:363274; -.
DR   AGR; RGD:1563955; -.
DR   CTD; 646960; -.
DR   RGD; 1563955; Prss56.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000157183; -.
DR   HOGENOM; CLU_034171_0_0_1; -.
DR   InParanoid; D3ZQJ8; -.
DR   OrthoDB; 4629979at2759; -.
DR   TreeFam; TF337807; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000029865; Expressed in heart and 2 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR   GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR   GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; ISO:RGD.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF10; SERINE PROTEASE 56; 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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..607
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003053169"
FT   DOMAIN          112..344
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          67..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  65597 MW;  54EA9AAA4CB80B3C CRC64;
     MPLAMLLLLL LLLLLSPDSQ TANGHPLYMR LSPSTLQVLS AQGTQALQAA QRSVQWAIKH
     VSMEIQHRRH ECQGPGRPRP QASVFQDPPP EPGPCGERRQ SVANTTRAHG RIVGGSTAPL
     GAWPWLVRLQ LGGLPLCGGV LVAASWVLTA AHCFAGASNE LLWTVMLAEG PQGEQAEEVQ
     VNRILPHPKF DPQTFHNDLA LVQLWTPVNS EGPARPICLP EGSREPPAGT PCTIAGWGAL
     FEDGPESEAV REARVPLLSA DTCQKALGPG LSPSTMLCAG YLAGGIDSCQ GDSGGPLTCS
     EPGPRPREVL FGVTSWGDGC GEPGKPGVYT RVAVFKDWLQ EQMSAGPSTR EPSCRELLNW
     NAREEEPFAD APGLCAFYER QCLGSESSCA RLALQQCVQR RRRCELRSLA HTLLGLLRGA
     QELLGPRPGL RRGAPAPAHS APSLQELPGH NAREQRLYSG SRVAGAWFQK PKQERRAETK
     GCPGLEPLQQ KLAAIQRAHA WILQIPAEHL AMNFHEVLAD LGSKTLTGLF RAWVRASLGD
     QRVVFSGLVG LEPSTLAQSL PRLLVQALKA FRSAFLTEGE PQASWIGTEQ EQRLGKEHQG
     QLQPPVP
//
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