ID   HG2A_MOUSE              Reviewed;         279 AA.
AC   P04441; O19452;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 3.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=H-2 class II histocompatibility antigen gamma chain {ECO:0000305};
DE   AltName: Full=Ia antigen-associated invariant chain;
DE            Short=Ii {ECO:0000303|PubMed:8977190};
DE            Short=Ii chain {ECO:0000303|PubMed:8977190};
DE   AltName: Full=MHC class II-associated invariant chain;
DE   AltName: CD_antigen=CD74;
DE   Contains:
DE     RecName: Full=Class-II-associated invariant chain peptide {ECO:0000250|UniProtKB:P04233};
DE              Short=CLIP {ECO:0000250|UniProtKB:P04233};
GN   Name=Cd74 {ECO:0000312|MGI:MGI:96534};
GN   Synonyms=Ii {ECO:0000303|PubMed:8977190};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND ALTERNATIVE SPLICING.
RC   STRAIN=AKR/J;
RX   PubMed=3038530; DOI=10.1002/j.1460-2075.1987.tb02417.x;
RA   Koch N., Lauer W., Habicht J., Dobberstein B.;
RT   "Primary structure of the gene for the murine Ia antigen-associated
RT   invariant chains (Ii). An alternatively spliced exon encodes a cysteine-
RT   rich domain highly homologous to a repetitive sequence of thyroglobulin.";
RL   EMBO J. 6:1677-1683(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AKR/J; TISSUE=Liver;
RX   PubMed=2492095; DOI=10.1093/nar/17.1.447;
RA   Zhu L., Jones P.P.;
RT   "Complete sequence of the murine invariant chain (Ii) gene.";
RL   Nucleic Acids Res. 17:447-448(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-58.
RC   TISSUE=Spleen;
RA   Stone J., Perry R., Todd J.A., McDevitt H.O.;
RT   "Nucleotide sequences of the murine Ia-associated invariant chain (Ii) and
RT   I-E (H-2S, Beta) chain expressible cDNA clones.";
RL   Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX   PubMed=2111346;
RA   Eades A.-M., Litfin M., Rahmsdorf H.J.;
RT   "The IFN-gamma response of the murine invariant chain gene is mediated by a
RT   complex enhancer that includes several MHC class II consensus elements.";
RL   J. Immunol. 144:4399-4409(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 47-279 (ISOFORM SHORT).
RX   PubMed=6327293; DOI=10.1002/j.1460-2075.1984.tb01899.x;
RA   Singer P.A., Lauer W., Dembic Z., Mayer W.E., Lipp J., Koch N.,
RA   Hammerling G., Klein J., Dobberstein B.;
RT   "Structure of the murine Ia-associated invariant (Ii) chain as deduced from
RT   a cDNA clone.";
RL   EMBO J. 3:873-877(1984).
RN   [7]
RP   GLYCOSYLATION AT SER-265, AND MUTAGENESIS OF SER-265.
RX   PubMed=3422739; DOI=10.1073/pnas.85.5.1359;
RA   Miller J., Hatch J.A., Simonis S., Cullen S.E.;
RT   "Identification of the glycosaminoglycan-attachment site of mouse
RT   invariant-chain proteoglycan core protein by site-directed mutagenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1359-1363(1988).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH CD44.
RX   PubMed=8343954; DOI=10.1016/0092-8674(93)90417-o;
RA   Naujokas M.F., Morin M., Anderson M.S., Peterson M., Miller J.;
RT   "The chondroitin sulfate form of invariant chain can enhance stimulation of
RT   T cell responses through interaction with CD44.";
RL   Cell 74:257-268(1993).
RN   [9]
RP   FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=8977190;
RA   Takaesu N.T., Lower J.A., Yelon D., Robertson E.J., Bikoff E.K.;
RT   "In vivo functions mediated by the p41 isoform of the MHC class II-
RT   associated invariant chain.";
RL   J. Immunol. 158:187-199(1997).
RN   [10]
RP   FUNCTION (LONG ISOFORM), TISSUE SPECIFICITY, INTERACTION WITH CTSL, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=11483509; DOI=10.1093/emboj/20.15.4055;
RA   Lennon-Dumenil A.M., Roberts R.A., Valentijn K., Driessen C.,
RA   Overkleeft H.S., Erickson A., Peters P.J., Bikoff E., Ploegh H.L.,
RA   Wolf Bryant P.;
RT   "The p41 isoform of invariant chain is a chaperone for cathepsin L.";
RL   EMBO J. 20:4055-4064(2001).
RN   [11]
RP   FUNCTION (LONG ISOFORM), TISSUE SPECIFICITY, INTERACTION WITH CTSL, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12417635; DOI=10.1084/jem.20020762;
RA   Fiebiger E., Maehr R., Villadangos J., Weber E., Erickson A., Bikoff E.,
RA   Ploegh H.L., Lennon-Dumenil A.M.;
RT   "Invariant chain controls the activity of extracellular cathepsin L.";
RL   J. Exp. Med. 196:1263-1269(2002).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [14]
RP   INDUCTION BY LPS.
RX   PubMed=32855215; DOI=10.1126/science.abb3753;
RA   Bruchez A., Sha K., Johnson J., Chen L., Stefani C., McConnell H.,
RA   Gaucherand L., Prins R., Matreyek K.A., Hume A.J., Muehlberger E.,
RA   Schmidt E.V., Olinger G.G., Stuart L.M., Lacy-Hulbert A.;
RT   "MHC class II transactivator CIITA induces cell resistance to Ebola virus
RT   and SARS-like coronaviruses.";
RL   Science 370:241-247(2020).
CC   -!- FUNCTION: Plays a critical role in MHC class II antigen processing by
CC       stabilizing peptide-free class II alpha/beta heterodimers in a complex
CC       soon after their synthesis and directing transport of the complex from
CC       the endoplasmic reticulum to compartments where peptide loading of
CC       class II takes place. Enhance also the stimulation of T-cell responses
CC       through interaction with CD44. {ECO:0000269|PubMed:8343954,
CC       ECO:0000269|PubMed:8977190}.
CC   -!- FUNCTION: [Isoform Long]: Stabilizes the conformation of mature CTSL by
CC       binding to its active site and serving as a chaperone to help maintain
CC       a pool of mature enzyme in endocytic compartments and extracellular
CC       space of antigen-presenting cells (APCs). {ECO:0000269|PubMed:11483509,
CC       ECO:0000269|PubMed:12417635}.
CC   -!- FUNCTION: [Class-II-associated invariant chain peptide]: Binds to the
CC       peptide-binding site of MHC class II alpha/beta heterodimers forming an
CC       alpha-beta-CLIP complex, thereby preventing the loading of antigenic
CC       peptides to the MHC class II complex until its release by HLA-DM in the
CC       endosome. {ECO:0000250|UniProtKB:P04233}.
CC   -!- SUBUNIT: Nonamer composed of three alpha/beta/gamma heterotrimers.
CC       Interacts with CD44; this complex is essential for the MIF-induced
CC       signaling cascade that results in B cell survival. {ECO:0000250,
CC       ECO:0000269|PubMed:8343954}.
CC   -!- SUBUNIT: [Isoform Long]: Interacts with the mature form of CTSL; the
CC       complex survive in neutral pH environment.
CC       {ECO:0000269|PubMed:11483509, ECO:0000269|PubMed:12417635}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Long]: Late endosome
CC       {ECO:0000269|PubMed:11483509}. Lysosome {ECO:0000269|PubMed:11483509}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04233};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:P04233}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04233}. Golgi
CC       apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P04233}. Endosome
CC       {ECO:0000250|UniProtKB:P04233}. Lysosome
CC       {ECO:0000250|UniProtKB:P04233}. Secreted
CC       {ECO:0000250|UniProtKB:P04233}. Note=Transits through a number of
CC       intracellular compartments in the endocytic pathway. It can either
CC       undergo proteolysis or reach the cell membrane.
CC       {ECO:0000250|UniProtKB:P04233}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long; Synonyms=p41 {ECO:0000303|PubMed:11483509,
CC       ECO:0000303|PubMed:12417635, ECO:0000303|PubMed:8977190};
CC         IsoId=P04441-1; Sequence=Displayed;
CC       Name=Short; Synonyms=p31 {ECO:0000303|PubMed:8977190};
CC         IsoId=P04441-2; Sequence=VSP_005332;
CC   -!- TISSUE SPECIFICITY: [Isoform Long]: Expressed in thymus and lymph
CC       noodes (PubMed:8977190). Expressed by antigen-presenting cells (APCs)
CC       (PubMed:11483509, PubMed:12417635). {ECO:0000269|PubMed:11483509,
CC       ECO:0000269|PubMed:12417635, ECO:0000269|PubMed:8977190}.
CC   -!- TISSUE SPECIFICITY: [Isoform Short]: Expressed in thymus and lymph
CC       noodes. {ECO:0000269|PubMed:8977190}.
CC   -!- INDUCTION: Expression is induced by IFNG and LPS, through CIITA.
CC       {ECO:0000269|PubMed:32855215}.
CC   -!- DISRUPTION PHENOTYPE: Mutants for Long isoform or Short isoform exhibit
CC       similar functional capabilities. {ECO:0000269|PubMed:8977190}.
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DR   EMBL; X05428; CAA29010.1; -; Genomic_DNA.
DR   EMBL; X05429; CAA29012.2; -; Genomic_DNA.
DR   EMBL; X05430; CAB37297.1; -; Genomic_DNA.
DR   EMBL; X13414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003476; AAH03476.1; -; mRNA.
DR   EMBL; X07129; CAA30141.1; -; mRNA.
DR   EMBL; M35872; AAA37897.1; -; Genomic_DNA.
DR   EMBL; X00496; CAA25191.1; -; mRNA.
DR   CCDS; CCDS37835.1; -. [P04441-1]
DR   CCDS; CCDS50299.1; -. [P04441-2]
DR   PIR; B27866; HLHMSG.
DR   RefSeq; NP_001036070.1; NM_001042605.1. [P04441-1]
DR   AlphaFoldDB; P04441; -.
DR   SMR; P04441; -.
DR   BioGRID; 200600; 2.
DR   CORUM; P04441; -.
DR   IntAct; P04441; 1.
DR   MINT; P04441; -.
DR   STRING; 10090.ENSMUSP00000095171; -.
DR   MEROPS; I31.002; -.
DR   GlyCosmos; P04441; 3 sites, No reported glycans.
DR   GlyGen; P04441; 3 sites.
DR   iPTMnet; P04441; -.
DR   PhosphoSitePlus; P04441; -.
DR   SwissPalm; P04441; -.
DR   EPD; P04441; -.
DR   PaxDb; 10090-ENSMUSP00000095171; -.
DR   PeptideAtlas; P04441; -.
DR   ProteomicsDB; 269741; -. [P04441-1]
DR   ProteomicsDB; 269742; -. [P04441-2]
DR   Antibodypedia; 2245; 2682 antibodies from 53 providers.
DR   DNASU; 16149; -.
DR   Ensembl; ENSMUST00000050487.16; ENSMUSP00000057836.9; ENSMUSG00000024610.16. [P04441-2]
DR   Ensembl; ENSMUST00000097563.9; ENSMUSP00000095171.3; ENSMUSG00000024610.16. [P04441-1]
DR   Ensembl; ENSMUST00000167610.2; ENSMUSP00000126688.2; ENSMUSG00000024610.16. [P04441-1]
DR   GeneID; 16149; -.
DR   KEGG; mmu:16149; -.
DR   UCSC; uc008faz.1; mouse. [P04441-1]
DR   AGR; MGI:96534; -.
DR   CTD; 972; -.
DR   MGI; MGI:96534; Cd74.
DR   VEuPathDB; HostDB:ENSMUSG00000024610; -.
DR   eggNOG; KOG1214; Eukaryota.
DR   GeneTree; ENSGT00390000008961; -.
DR   HOGENOM; CLU_086066_1_0_1; -.
DR   InParanoid; P04441; -.
DR   OMA; HHNCSEP; -.
DR   OrthoDB; 2972165at2759; -.
DR   PhylomeDB; P04441; -.
DR   TreeFam; TF317779; -.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   BioGRID-ORCS; 16149; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Cd74; mouse.
DR   PRO; PR:P04441; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P04441; Protein.
DR   Bgee; ENSMUSG00000024610; Expressed in spleen and 59 other cell types or tissues.
DR   ExpressionAtlas; P04441; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0042613; C:MHC class II protein complex; IDA:BHF-UCL.
DR   GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR   GO; GO:0035693; C:NOS2-CD74 complex; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005773; C:vacuole; ISO:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0042609; F:CD4 receptor binding; ISO:MGI.
DR   GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR   GO; GO:0004896; F:cytokine receptor activity; IMP:BHF-UCL.
DR   GO; GO:0035718; F:macrophage migration inhibitory factor binding; ISO:MGI.
DR   GO; GO:0042289; F:MHC class II protein binding; IPI:BHF-UCL.
DR   GO; GO:0042658; F:MHC class II protein binding, via antigen binding groove; ISO:MGI.
DR   GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI.
DR   GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR   GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR   GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:MGI.
DR   GO; GO:0006952; P:defense response; IMP:MGI.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR   GO; GO:0035691; P:macrophage migration inhibitory factor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR   GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
DR   GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IMP:BHF-UCL.
DR   GO; GO:0002792; P:negative regulation of peptide secretion; ISO:MGI.
DR   GO; GO:0045581; P:negative regulation of T cell differentiation; IMP:MGI.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR   GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR   GO; GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR   GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IDA:BHF-UCL.
DR   GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR   GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0045089; P:positive regulation of innate immune response; IC:BHF-UCL.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:BHF-UCL.
DR   GO; GO:2000448; P:positive regulation of macrophage migration inhibitory factor signaling pathway; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR   GO; GO:0045657; P:positive regulation of monocyte differentiation; ISO:MGI.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
DR   GO; GO:0002830; P:positive regulation of type 2 immune response; IMP:BHF-UCL.
DR   GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:MGI.
DR   GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0070206; P:protein trimerization; IEA:InterPro.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:MGI.
DR   GO; GO:0034341; P:response to type II interferon; IDA:UniProtKB.
DR   GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 1.10.870.10; MHC class II-associated invariant chain, trimerisation domain; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 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   PANTHER; PTHR14093; HLA CLASS II GAMMA CHAIN; 1.
DR   PANTHER; PTHR14093:SF17; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN; 1.
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; Class II MHC-associated invariant chain ectoplasmic trimerization domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR   Genevisible; P04441; MM.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Alternative splicing; Cell membrane; Chaperone;
KW   Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
KW   Golgi apparatus; Immunity; Lysosome; Membrane; Phosphoprotein;
KW   Proteoglycan; Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..279
FT                   /note="H-2 class II histocompatibility antigen gamma chain"
FT                   /id="PRO_0000067955"
FT   PEPTIDE         80..103
FT                   /note="Class-II-associated invariant chain peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P04233"
FT                   /id="PRO_0000448887"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..55
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          193..254
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:3422739"
FT   DISULFID        196..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        226..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        235..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   VAR_SEQ         192..255
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:6327293"
FT                   /id="VSP_005332"
FT   MUTAGEN         265
FT                   /note="S->A: No addition of glycosaminoglycan; no effect on
FT                   the synthesis of the protein."
FT                   /evidence="ECO:0000269|PubMed:3422739"
FT   CONFLICT        10
FT                   /note="N -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="N -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229..231
FT                   /note="STG -> RHC (in Ref. 1; CAB37297)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  31557 MW;  300A85014F170792 CRC64;
     MDDQRDLISN HEQLPILGNR PREPERCSRG ALYTGVSVLV ALLLAGQATT AYFLYQQQGR
     LDKLTITSQN LQLESLRMKL PKSAKPVSQM RMATPLLMRP MSMDNMLLGP VKNVTKYGNM
     TQDHVMHLLT RSGPLEYPQL KGTFPENLKH LKNSMDGVNW KIFESWMKQW LLFEMSKNSL
     EEKKPTEAPP KVLTKCQEEV SHIPAVYPGA FRPKCDENGN YLPLQCHGST GYCWCVFPNG
     TEVPHTKSRG RHNCSEPLDM EDLSSGLGVT RQELGQVTL
//