ID A0A1S3EUG5_DIPOR Unreviewed; 1129 AA.
AC A0A1S3EUG5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=MHC class II transactivator isoform X1 {ECO:0000313|RefSeq:XP_012867052.1};
GN Name=Ciita {ECO:0000313|RefSeq:XP_012867052.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012867052.1};
RN [1] {ECO:0000313|RefSeq:XP_012867052.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012867052.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_012867052.1; XM_013011598.1.
DR AlphaFoldDB; A0A1S3EUG5; -.
DR STRING; 10020.ENSDORP00000002129; -.
DR GeneID; 105982132; -.
DR KEGG; dord:105982132; -.
DR CTD; 4261; -.
DR InParanoid; A0A1S3EUG5; -.
DR OrthoDB; 5311112at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00116; LRR_RI; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR008095; MHC_II_transact.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47189; MHC CLASS II TRANSACTIVATOR; 1.
DR PANTHER; PTHR47189:SF1; MHC CLASS II TRANSACTIVATOR; 1.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF05729; NACHT; 1.
DR PRINTS; PR01719; MHCIIACTVATR.
DR SMART; SM00368; LRR_RI; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT DOMAIN 415..550
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 122366 MW; F6C8D8EE27822D76 CRC64;
MRCLAPCPLG PHLPEPQGSG QPGTMEVGLP EGGYLELLNS DTDPLCLYHI CDQMDLAGEE
IELCSEADPE TINCDQFTRL LCDVEEDEEA GEAYANIAEL DQYVFQDSQM EGLSKDIFIE
HIGLDEGTCE SVEVPAEVGK RNQKRSLPEE QPLDPKRRKP AETPAVPILT GSFLVGPVGS
NSPLLCPSPA LFSQEPVPGQ APLEGAVQLT ALPSGSSMNC FHLSAGPFQF ISTLPALPQG
CWQISESGTN ISGIFIYHGD IPQASQVFPC PGPPVQSLPK SPERPGSTSP FAPSTADLPS
MPEAALTSRA GVTEDDMSPS PHQGAAEVSV SLPKWPGPVE QFCRSLRDRY QAEPAGLDGL
LVDVDLVRAR LEKGSNKSQE RELATLDWAE RQPAHGGLAE VLLSTRDRRQ PRETHVIAVL
GKAGVGKSHW ARAVSRAWAC GQLPQYDFVF HVPCHCLDRP GTTYRLQDLL CPAGLHAQAL
DDRILSHIVR RSNHVLLILD GFEELEAQDG SCGPVCSEPC SFRGLLAGLF QGKLLRGCTL
VLTARPRGRL AQCLSKADAL FEVPGFSAEQ ALTYLRRYFE DTGATEDQER ALVLLREQPF
LSSHGHNPAV CQAVCQLSKV LLRAGAEAQL PCTLTGLYVG LVGPAARDSP PGALASLAEL
AWELGRRHQS TLREDQFPSA EVRTWAVARG LVRAAPGAVE AGLAFASFPL HCFLGALWLA
QSSDIKDKKL PQYLALTPRK KRPYDNWLAG APRFLVGLLF QPRARCLGAL LGPAAAAATG
ADRKRKVLTR YLKRLQPGKL QAARVLELLH CAHEAQDPGI WQHVLQGLPE HLSFLGTRLT
PPDAHLLGRA LESAGRDFSL DLRSTGLDPS GLGSLVGLSC VTRFRAALSD TTGLWESLRR
RGETPLLCAA EEKFTIEPFK AKSLKDVEDL GHLVQTPRVT RCSDDPARDL PAVRDLKKLE
FALGPVLGAQ AFPKLARILP AFSSLQHLDL DSLSENKIGD EGVAQLSATF PWLKALETLN
LSQNSITDVG ACQLADALPA LAATLLRLSL YNNCICDKGA ESLARVLPDM ESLRVMDVQY
NKFTAVGAQQ LAASLRKCPH LHTLAMWTPT IPFGVQEHLQ QLDSRISLR
//