HG2A_MOUSE
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 03-AUG-2022, entry version 205.
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}. 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 BioGRID; 200600; 1.
DR CORUM; P04441; -.
DR IntAct; P04441; 1.
DR MINT; P04441; -.
DR STRING; 10090.ENSMUSP00000095171; -.
DR MEROPS; I31.002; -.
DR GlyGen; P04441; 3 sites.
DR iPTMnet; P04441; -.
DR PhosphoSitePlus; P04441; -.
DR SwissPalm; P04441; -.
DR EPD; P04441; -.
DR PaxDb; P04441; -.
DR PeptideAtlas; P04441; -.
DR PRIDE; P04441; -.
DR ProteomicsDB; 269741; -. [P04441-1]
DR ProteomicsDB; 269742; -. [P04441-2]
DR Antibodypedia; 2245; 2388 antibodies from 53 providers.
DR DNASU; 16149; -.
DR Ensembl; ENSMUST00000050487; ENSMUSP00000057836; ENSMUSG00000024610. [P04441-2]
DR Ensembl; ENSMUST00000097563; ENSMUSP00000095171; ENSMUSG00000024610. [P04441-1]
DR Ensembl; ENSMUST00000167610; ENSMUSP00000126688; ENSMUSG00000024610. [P04441-1]
DR GeneID; 16149; -.
DR KEGG; mmu:16149; -.
DR UCSC; uc008faz.1; mouse. [P04441-1]
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; GTFRPQC; -.
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 76 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 56 other tissues.
DR ExpressionAtlas; P04441; baseline and differential.
DR Genevisible; P04441; MM.
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:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS: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: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:0008283; P:cell population proliferation; ISO: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: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: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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; 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:0033674; P:positive regulation of kinase activity; 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:0045893; P:positive regulation of transcription, DNA-templated; ISO: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 interferon-gamma; 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; -; 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 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; 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
