ID HG2A_HUMAN STANDARD; PRT; 296 AA. AC P04233; Q14597; Q29832; Q8WLP6; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 3. DT 04-APR-2006, entry version 76. DE HLA class II histocompatibility antigen gamma chain (HLA-DR antigens- DE associated invariant chain) (Ia antigen-associated invariant chain) DE (Ii) (p33) (CD74 antigen). GN Name=CD74; Synonyms=DHLAG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=84207945; PubMed=6586420; RA Strubin M., Mach B., Long E.O.; RT "The complete sequence of the mRNA for the HLA-DR-associated invariant RT chain reveals a polypeptide with an unusual transmembrane polarity."; RL EMBO J. 3:869-872(1984). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=86093681; PubMed=3001652; RA Kudo J., Chao L.-Y., Narni F., Saunders G.F.; RT "Structure of the human gene encoding the invariant gamma-chain of RT class II histocompatibility antigens."; RL Nucleic Acids Res. 13:8827-8841(1985). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORMS LONG AND SHORT). RC TISSUE=Liver; RX MEDLINE=86233451; PubMed=3459184; RA O'Sullivan D.M., Larhammar D., Wilson M.C., Peterson P.A., RA Quaranta V.; RT "Structure of the human Ia-associated invariant (gamma)-chain gene: RT identification of 5' sequences shared with major histocompatibility RT complex class II genes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4484-4488(1986). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC TISSUE=Tonsil; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE OF 27-96. RX MEDLINE=84170234; PubMed=6324166; RA Claesson L., Larhammar D., Rask L., Peterson P.A.; RT "cDNA clone for the human invariant gamma chain of class II RT histocompatibility antigens and its implications for the protein RT structure."; RL Proc. Natl. Acad. Sci. U.S.A. 80:7395-7399(1983). RN [6] RP PROTEIN SEQUENCE OF 97-120. RX MEDLINE=93078879; PubMed=1448172; DOI=10.1038/360474a0; RA Riberdy J.M., Newcomb J.R., Surman M.J., Barbosa J.A., Cresswell P.; RT "HLA-DR molecules from an antigen-processing mutant cell line are RT associated with invariant chain peptides."; RL Nature 360:474-477(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 103-117. RX MEDLINE=96085023; PubMed=7477400; DOI=10.1038/378457a0; RA Ghosh P., Amaya M., Mellins E., Wiley D.C.; RT "The structure of an intermediate in class II MHC maturation: CLIP RT bound to HLA-DR3."; RL Nature 378:457-462(1995). RN [8] RP STRUCTURE BY NMR OF 134-208. RX MEDLINE=99059718; PubMed=9843486; DOI=10.1093/emboj/17.23.6812; RA Jasanoff A., Wagner G., Wiley D.C.; RT "Structure of a trimeric domain of the MHC class II-associated RT chaperonin and targeting protein Ii."; RL EMBO J. 17:6812-6818(1998). CC -!- FUNCTION: Plays a critical role in MHC class II antigen processing CC by stabilizing peptide-free class II alpha/beta heterodimers in a CC complex soon after their synthesis and directing transport of the CC complex from the endoplasmic reticulum to compartments where CC peptide loading of class II takes place. CC -!- SUBUNIT: Nonamer composed of three alpha/beta/gamma heterotrimers. CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P04233-1; Sequence=Displayed; CC Name=Short; CC IsoId=P04233-2; Sequence=VSP_005331; CC -!- SIMILARITY: Contains 1 thyroglobulin type-1 domain. 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 EMBL; K01144; AAA36304.1; -; mRNA. DR EMBL; X03339; CAA27046.1; -; Genomic_DNA. DR EMBL; X03340; CAA27047.1; -; Genomic_DNA. DR EMBL; X00497; CAA25192.1; -; mRNA. DR EMBL; X00497; CAA25193.1; -; mRNA. DR EMBL; M13560; AAA36033.1; -; Genomic_DNA. DR EMBL; M13555; AAA36033.1; JOINED; Genomic_DNA. DR EMBL; M13556; AAA36033.1; JOINED; Genomic_DNA. DR EMBL; M13558; AAA36033.1; JOINED; Genomic_DNA. DR EMBL; M13559; AAA36033.1; JOINED; Genomic_DNA. DR EMBL; BC018726; AAH18726.1; -; mRNA. DR PIR; A93981; HLHUG. DR UniGene; Hs.436568; -. DR PDB; 1A6A; X-ray; C=103-117. DR PDB; 1ICF; X-ray; I/J=210-274. DR PDB; 1IIE; NMR; A/B/C=134-208. DR PDB; 1L3H; NMR; A=210-274. DR Ensembl; ENSG00000019582; Homo sapiens. DR H-InvDB; HIX0005314; -. DR HGNC; HGNC:1697; CD74. DR MIM; 142790; gene. DR LinkHub; P04233; -. DR GO; GO:0016021; C:integral to membrane; TAS. DR GO; GO:0005622; C:intracellular; TAS. DR GO; GO:0019955; F:cytokine binding; IPI. DR GO; GO:0042802; F:identical protein binding; TAS. DR GO; GO:0042289; F:MHC class II protein binding; NAS. DR GO; GO:0019883; P:antigen presentation, endogenous antigen; NAS. DR GO; GO:0008283; P:cell proliferation; IDA. DR GO; GO:0016064; P:humoral defense mechanism (sensu Vertebrata); ISS. DR GO; GO:0006886; P:intracellular protein transport; ISS. DR GO; GO:0043066; P:negative regulation of apoptosis; IDA. DR GO; GO:0001516; P:prostaglandin biosynthesis; IDA. DR GO; GO:0006461; P:protein complex assembly; ISS. DR GO; GO:0043030; P:regulation of macrophage activation; NAS. DR GO; GO:0007165; P:signal transduction; IDA. DR GO; GO:0045058; P:T cell selection; NAS. DR InterPro; IPR011988; MHCII_invariant. DR InterPro; IPR000716; Thyroglobulin_1. DR Pfam; PF00086; Thyroglobulin_1; 1. DR SMART; SM00211; TY; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1. KW 3D-structure; Alternative splicing; Chaperone; KW Direct protein sequencing; Glycoprotein; Immune response; Membrane; KW Proteoglycan; Signal-anchor; Transmembrane. FT CHAIN 1 296 HLA class II histocompatibility antigen FT gamma chain. FT /FTId=PRO_0000067954. FT TOPO_DOM 1 46 Cytoplasmic (Potential). FT TRANSMEM 47 72 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 73 296 Extracellular (Potential). FT DOMAIN 210 271 Thyroglobulin type-1. FT REGION 103 117 CLIP. FT CARBOHYD 130 130 N-linked (GlcNAc...). FT CARBOHYD 136 136 N-linked (GlcNAc...). FT CARBOHYD 282 282 O-linked (Xyl...) (glycosaminoglycan) FT (Potential). FT DISULFID 213 232 By similarity. FT DISULFID 243 250 By similarity. FT DISULFID 252 271 By similarity. FT VARSPLIC 209 272 Missing (in isoform Short). FT /FTId=VSP_005331. FT CONFLICT 167 167 R -> T (in Ref. 2). FT STRAND 105 106 FT STRAND 136 137 FT HELIX 139 149 FT TURN 151 152 FT STRAND 160 160 FT HELIX 162 172 FT STRAND 173 173 FT HELIX 175 194 FT TURN 195 195 FT STRAND 198 199 FT STRAND 206 206 FT HELIX 212 217 FT TURN 218 219 FT STRAND 220 220 FT STRAND 222 223 FT TURN 225 226 FT STRAND 232 232 FT TURN 234 235 FT STRAND 236 236 FT STRAND 238 238 FT STRAND 240 244 FT TURN 245 248 FT STRAND 249 253 FT TURN 255 256 FT STRAND 257 257 FT STRAND 259 259 FT TURN 261 262 FT STRAND 265 267 SQ SEQUENCE 296 AA; 33516 MW; 27A13F252D5FB91D CRC64; MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY TGFSILVTLL LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP PKPVSKMRMA TPLLMQALPM GALPQGPMQN ATKYGNMTED HVMHLLQNAD PLKVYPPLKG SFPENLRHLK NTMETIDWKV FESWMHHWLL FEMSRHSLEQ KPTDAPPKVL TKCQEEVSHI PAVHPGSFRP KCDENGNYLP LQCYGSIGYC WCVFPNGTEV PNTRSRGHHN CSESLELEDP SSGLGVTKQD LGPVPM //