ID A0A8J0QFG2_XENLA Unreviewed; 292 AA. AC A0A8J0QFG2; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 03-AUG-2022, entry version 2. DE SubName: Full=CD74 molecule, major histocompatibility complex, class II invariant chain {ECO:0000313|RefSeq:NP_001184041.1}; GN Name=cd74.S {ECO:0000313|RefSeq:NP_001184041.1}; GN Synonyms=cd74 {ECO:0000313|RefSeq:NP_001184041.1}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:NP_001184041.1}; RN [1] {ECO:0000313|RefSeq:NP_001184041.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12454917; DOI=10.1002/dvdy.10174; RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W., RA Richardson P.; RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus RT initiative."; RL Dev. Dyn. 225:384-391(2002). RN [2] {ECO:0000313|RefSeq:NP_001184041.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2022) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; NP_001184041.1; NM_001197112.1. DR Proteomes; UP000186698; Chromosome 3S. DR CDD; cd00191; TY; 1. DR Gene3D; 1.10.870.10; -; 1. DR Gene3D; 4.10.800.10; -; 1. DR InterPro; IPR043530; CD74_antigen. DR InterPro; IPR015386; MHC_II-assoc_invar/CLIP_MHC-bd. DR InterPro; IPR022339; MHC_II-assoc_invar_chain. DR InterPro; IPR011988; MHC_II-assoc_invariant_trimer. DR InterPro; IPR036613; MHCII_invariant_trimer_sf. DR InterPro; IPR000716; Thyroglobulin_1. DR InterPro; IPR036857; Thyroglobulin_1_sf. DR Pfam; PF09307; MHC2-interact; 1. DR Pfam; PF08831; MHCassoc_trimer; 1. DR Pfam; PF00086; Thyroglobulin_1; 1. DR PIRSF; PIRSF001992; CD74_antigen; 1. DR PRINTS; PR01990; CD74ANTIGEN. DR SMART; SM00211; TY; 1. DR SUPFAM; SSF48305; SSF48305; 1. DR SUPFAM; SSF57610; SSF57610; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1. PE 4: Predicted; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00500}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000186698}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35..57 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 207..266 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000259|PROSITE:PS51162" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 238..245 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500" SQ SEQUENCE 292 AA; 32926 MW; CF72CD8865766A10 CRC64; MAEESQNLVP EHVPGQSVVD VGNGERRMSC NKGSLVTALT VLVAVLVAGQ AVMAFFITQQ NSRIQDLDRS TKNLQLKAMM KELPGSPPVP SKQKMRTFNI PMALKLYDGS EMNMNDLEQM AQTGNKMEDA AKYMLLRGNP LRKYPSLNGT ILENLRELKK TLTDQEWMTF DAWMQQWYLF FLVQNTEKPA EPLPSTKNTA VTGAPLMTEC QTLSRIHTMT GTYKPQCEQN GDFKPLQCWP STGFCWCVYH NGTEIPETRT RSRLDCSSIM QPEDPMFLES ITSSDADFGP FD //