UniProt: D4A980

Database: UniProt
Entry: D4A980_RAT

LinkDB:  D4A980_RAT 
Original site:  D4A980_RAT

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Ontology (34)   
   GO (34)   
Gene (5)   
   KEGG GENES (1)   
   ENSEMBL-UP (3)   
   RGD (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (20)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (62)   

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ID   D4A980_RAT              Unreviewed;       832 AA.
AC   D4A980;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=MALT1 paracaspase {ECO:0000313|Ensembl:ENSRNOP00000059281.3};
GN   Name=Malt1 {ECO:0000313|Ensembl:ENSRNOP00000059281.3,
GN   ECO:0000313|RGD:1309195};
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:ENSRNOP00000059281.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000059281.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000059281.3,
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:ENSRNOP00000059281.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000059281.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_003751846.1; XM_003751798.4.
DR   RefSeq; XP_003753105.1; XM_003753057.4.
DR   AlphaFoldDB; D4A980; -.
DR   STRING; 10116.ENSRNOP00000059281; -.
DR   jPOST; D4A980; -.
DR   PaxDb; 10116-ENSRNOP00000059281; -.
DR   Ensembl; ENSRNOT00000068418.5; ENSRNOP00000059281.3; ENSRNOG00000017181.9.
DR   KEGG; rno:307366; -.
DR   UCSC; RGD:1309195; rat.
DR   AGR; RGD:1309195; -.
DR   CTD; 10892; -.
DR   RGD; 1309195; Malt1.
DR   VEuPathDB; HostDB:ENSRNOG00000017181; -.
DR   eggNOG; ENOG502QUZM; Eukaryota.
DR   GeneTree; ENSGT00390000018044; -.
DR   HOGENOM; CLU_014796_0_0_1; -.
DR   InParanoid; D4A980; -.
DR   OMA; CLMSDGP; -.
DR   TreeFam; TF319744; -.
DR   Reactome; R-RNO-202424; Downstream TCR signaling.
DR   Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-RNO-5660668; CLEC7A/inflammasome pathway.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000017181; Expressed in spleen and 19 other cell types or tissues.
DR   GO; GO:0032449; C:CBM complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0002096; C:polkadots; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR   GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR   GO; GO:0002020; F:protease binding; ISO:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:0036094; F:small molecule binding; ISO:RGD.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR   GO; GO:0042113; P:B cell activation; ISO:RGD.
DR   GO; GO:0001923; P:B-1 B cell differentiation; ISO:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; ISO:RGD.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0051168; P:nuclear export; ISO:RGD.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR   GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
DR   GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:RGD.
DR   GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; ISO:RGD.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:RGD.
DR   GO; GO:0009620; P:response to fungus; ISO:RGD.
DR   GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR   CDD; cd08783; Death_MALT1; 1.
DR   CDD; cd00096; Ig; 2.
DR   Gene3D; 2.60.40.3360; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR037940; MALT1_Death.
DR   InterPro; IPR041077; MALT1_Ig.
DR   InterPro; IPR033540; MALT1_IG-like_dom_sf.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   PANTHER; PTHR22576; MUCOSA ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1/PARACASPASE; 1.
DR   PANTHER; PTHR22576:SF40; MUCOSA-ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF18703; MALT1_Ig; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50208; CASPASE_P20; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          131..207
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          236..314
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          349..427
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  92951 MW;  65100297A41CFFE9 CRC64;
     MSLWGQPLQA SPPPAVQQPL TASSGPSTAP PAGSTLNRLP EPLLRRLSES LDRAPEGRGW
     RQLAELAGSR GRLRLSCLDL EQCSLKVLEP EGSPSLCLLK LMGEKGCTVP ELSDFLQALE
     HTEVLQLLNP PGLKITVNPE SKAVLAGQFV KLCCRATGHP FVQYQWFKMN KEIPYGNSSE
     LIFNTVHVKD AGFYVCRVNN NSTFEFSQWS QLDVCDVTEV SDSFQGSLDG VSESKLRICV
     EPQSQKLAPG SALLLQCVAI GSPVPHYQWF KDESPLAHET KKHYTVPYVD LEHEGTYWCH
     VYNDRDSQDS KKVEIIIGRT DGAVECTEDE LNNLGRPDNK EQTGQPLAKD KVALLIGNMN
     YWEHPKLKAP LVDVYELTNL LRQLDFKVVS LLDLTEYEMC NAVDEFLLLL DKGVYGLLYY
     AGHGYENFGN SFMVPVDAPN PYRSENCLCV QNILKLMQEK ETGLNVFLLD MCRKRNDYDD
     TIPILDALKV TANIVFGYAT CQGAEAFEIQ HSGLANGIFM KFLKDRLLED KKITVLLDEV
     AEDMGKCHLT KGRQALEIRS SLSEKRALTD PIQGAPCSAE ALVRNLQWAK AHELPESMCL
     KFQCGVHIQL GFAAEFSNVM IIYTSIVHKP PEIIMCDAYV TDFPLDLDID PKHANKGTPE
     ETGSYLVSKE LPKHCLYTRL SSLQKLKEHL IFTVCLSYQY SGLEDTVEEK QEVSVGKPLI
     AKLDMHRGLG RKTCLQACPM PDETCHSSTS TSAGAGHFHS SQDSFHDVYH SQLGNSDSAM
     PPDRCHCSRT PHAFISNYPP HHYCQFGRSN VPVETTDEMP FSFSDRLMIS EN
//

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