ID HG2A_HUMAN Reviewed; 296 AA. AC P04233; A8K7R1; B4DNE8; D3DQG3; D3DQG4; Q14597; Q29832; Q5U0J8; Q8SNA0; AC Q8WLP6; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 3. DT 28-JUN-2023, entry version 236. DE RecName: Full=HLA class II histocompatibility antigen gamma chain {ECO:0000305}; DE AltName: Full=HLA-DR antigens-associated invariant chain; DE AltName: Full=Ia antigen-associated invariant chain; DE Short=Ii; DE AltName: CD_antigen=CD74; DE Contains: DE RecName: Full=Class-II-associated invariant chain peptide {ECO:0000303|PubMed:1448172}; DE Short=CLIP {ECO:0000303|PubMed:1448172}; GN Name=CD74 {ECO:0000312|HGNC:HGNC:1697}; Synonyms=DHLAG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P35). RX PubMed=6324166; DOI=10.1073/pnas.80.24.7395; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P35). RX PubMed=6586420; DOI=10.1002/j.1460-2075.1984.tb01898.x; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM P35). RX PubMed=3001652; DOI=10.1093/nar/13.24.8827; RA Kudo J., Chao L.-Y., Narni F., Saunders G.F.; RT "Structure of the human gene encoding the invariant gamma-chain of class II RT histocompatibility antigens."; RL Nucleic Acids Res. 13:8827-8841(1985). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS P45 RP AND P35). RC TISSUE=Liver; RX PubMed=3459184; DOI=10.1073/pnas.83.12.4484; RA O'Sullivan D.M., Larhammar D., Wilson M.C., Peterson P.A., Quaranta V.; RT "Structure of the human Ia-associated invariant (gamma)-chain gene: RT identification of 5' sequences shared with major histocompatibility complex RT class II genes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4484-4488(1986). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P35). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P45 AND P35). RC TISSUE=Heart, and Synovium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P35 AND 3). RC TISSUE=B-cell, and Tonsil; 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 [10] RP PROTEIN SEQUENCE OF 22-35; 81-94; 171-179 AND 273-288, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [11] RP PROTEIN SEQUENCE OF 97-120, AND FUNCTION. RX 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 [12] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=3104027; DOI=10.1002/j.1460-2075.1986.tb04673.x; RA Strubin M., Berte C., Mach B.; RT "Alternative splicing and alternative initiation of translation explain the RT four forms of the Ia antigen-associated invariant chain."; RL EMBO J. 5:3483-3488(1986). RN [13] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1. RX PubMed=12661006; DOI=10.1002/gcc.10207; RA Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H., RA Housman D.; RT "Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with RT an interstitial del(6)(q21q21)."; RL Genes Chromosomes Cancer 37:58-71(2003). RN [14] RP INTERACTION WITH MIF. RX PubMed=12782713; DOI=10.1084/jem.20030286; RA Leng L., Metz C.N., Fang Y., Xu J., Donnelly S., Baugh J., Delohery T., RA Chen Y., Mitchell R.A., Bucala R.; RT "MIF signal transduction initiated by binding to CD74."; RL J. Exp. Med. 197:1467-1476(2003). RN [15] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP GLYCOSYLATION AT THR-203, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.m111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of N- and RT O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 11:1-17(2012). RN [19] RP GLYCOSYLATION AT THR-203 AND SER-281, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=23234360; DOI=10.1021/pr300963h; RA Halim A., Ruetschi U., Larson G., Nilsson J.; RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures RT of human cerebrospinal fluid glycoproteins."; RL J. Proteome Res. 12:573-584(2013). RN [20] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-282. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP GLYCOSYLATION AT SER-282. RX PubMed=32337544; DOI=10.1093/glycob/cwaa039; RA Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A., RA Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D., RA Larson G., Salanti A., Clausen T.M.; RT "An affinity chromatography and glycoproteomics workflow to profile the RT chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in RT the placenta and in cancer."; RL Glycobiology 30:989-1002(2020). RN [23] RP FUNCTION (ISOFORM P41), ALTERNATIVE SPLICING, AND MUTAGENESIS OF RP 225-PRO-GLY-226. 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). RN [24] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-282. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 103-117 (CLIP) IN COMPLEX WITH RP HLA-DRA/HLA-DRB1 HETERODIMER. RX 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 bound to RT HLA-DR3."; RL Nature 378:457-462(1995). RN [26] RP STRUCTURE BY NMR OF 134-208. RX 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 chaperonin RT and targeting protein Ii."; RL EMBO J. 17:6812-6818(1998). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 210-274, GLYCOSYLATION AT ASN-256, RP DISULFIDE BONDS, AND INTERACTION WITH CTSL. RX PubMed=10022822; DOI=10.1093/emboj/18.4.793; RA Guncar G., Pungercic G., Klemencic I., Turk V., Turk D.; RT "Crystal structure of MHC class II-associated p41 Ii fragment bound to RT cathepsin L reveals the structural basis for differentiation between RT cathepsins L and S."; RL EMBO J. 18:793-803(1999). 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 the endosomal/lysosomal system where the CC antigen processing and binding of antigenic peptides to MHC class II CC takes place. Serves as cell surface receptor for the cytokine MIF. 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:0000269|PubMed:1448172}. CC -!- FUNCTION: [Isoform p41]: 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). Has antiviral activity by CC stymieing the endosomal entry of Ebola virus and coronaviruses, CC including SARS-CoV-2 (PubMed:32855215). Disrupts cathepsin-mediated CC Ebola virus glycoprotein processing, which prevents viral fusion and CC entry. This antiviral activity is specific to p41 isoform CC (PubMed:32855215). {ECO:0000250|UniProtKB:P04441, CC ECO:0000269|PubMed:32855215}. CC -!- SUBUNIT: Homotrimer. In the endoplasmic reticulum (ER) it forms a CC heterononameric MHC II-Ii complex: 3 MHC class II molecules CC (heterodimers of an alpha and a beta subunit) bind to the CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the endosomal/lysosomal CC system, the CD74 component undergoes sequential degradation by various CC proteases, including CTSS and CTSL, leaving a small fragment termed CC CLIP (class-II-associated invariant chain peptide) attached to the MHC CC class II molecule (alpha-beta-CLIP complex). This processed complex CC interacts with HLA_DM and HLA_DO heterodimers in order to release CLIP CC and facilitate the binding of antigenic peptides to the MHC class II CC molecules. Interacts with CD44; this complex is essential for the MIF- CC induced signaling cascade that results in B cell survival. CC {ECO:0000250|UniProtKB:P04441, ECO:0000269|PubMed:12782713, CC ECO:0000269|PubMed:7477400}. CC -!- SUBUNIT: [Isoform p41]: Interacts with the mature form of CTSL; the CC complex survive in neutral pH environment. CC {ECO:0000269|PubMed:10022822}. CC -!- INTERACTION: CC P04233; P16070: CD44; NbExp=9; IntAct=EBI-2622890, EBI-490245; CC P04233; P25025: CXCR2; NbExp=2; IntAct=EBI-2622890, EBI-2835281; CC P04233; P61073: CXCR4; NbExp=4; IntAct=EBI-2622890, EBI-489411; CC P04233; P60228: EIF3E; NbExp=2; IntAct=EBI-2622890, EBI-347740; CC P04233; Q14974: KPNB1; NbExp=2; IntAct=EBI-2622890, EBI-286758; CC P04233; P0A6Y8: dnaK; Xeno; NbExp=8; IntAct=EBI-2622890, EBI-542092; CC P04233-2; O15155: BET1; NbExp=3; IntAct=EBI-12222807, EBI-749204; CC P04233-2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12222807, EBI-12256978; CC P04233-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12222807, EBI-11989440; CC P04233-2; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-12222807, EBI-2807956; CC P04233-2; P56851: EDDM3B; NbExp=3; IntAct=EBI-12222807, EBI-10215665; CC P04233-2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12222807, EBI-711490; CC P04233-2; P37268: FDFT1; NbExp=3; IntAct=EBI-12222807, EBI-714550; CC P04233-2; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12222807, EBI-713304; CC P04233-2; Q9UBY5: LPAR3; NbExp=4; IntAct=EBI-12222807, EBI-12033434; CC P04233-2; Q8N912: NRAC; NbExp=4; IntAct=EBI-12222807, EBI-12051377; CC P04233-2; P0DJD7: PGA4; NbExp=3; IntAct=EBI-12222807, EBI-12957629; CC P04233-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12222807, EBI-12188331; CC P04233-2; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-12222807, EBI-10485931; CC P04233-2; Q8WZA1: POMGNT1; NbExp=3; IntAct=EBI-12222807, EBI-3912424; CC P04233-2; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-12222807, EBI-14199621; CC P04233-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12222807, EBI-10244780; CC P04233-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12222807, EBI-8652744; CC P04233-2; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-12222807, EBI-10329948; CC P04233-2; P78383: SLC35B1; NbExp=3; IntAct=EBI-12222807, EBI-12147661; CC P04233-2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12222807, EBI-12188413; CC P04233-2; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-12222807, EBI-11523345; CC P04233-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-12222807, EBI-10171534; CC P04233-2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-12222807, EBI-12887458; CC P04233-2; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-12222807, EBI-11956809; CC P04233-2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12222807, EBI-2852148; CC P04233-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12222807, EBI-12111910; CC P04233-2; O00526: UPK2; NbExp=4; IntAct=EBI-12222807, EBI-10179682; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane. Golgi CC apparatus, trans-Golgi network. Endosome. Lysosome. Secreted CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313}. CC Note=Transits through a number of intracellular compartments in the CC endocytic pathway. It can either undergo proteolysis or reach the cell CC membrane. CC -!- SUBCELLULAR LOCATION: [Isoform p41]: Late endosome CC {ECO:0000250|UniProtKB:P04441}. Lysosome CC {ECO:0000250|UniProtKB:P04441}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=p45 {ECO:0000303|PubMed:3104027}; Synonyms=Long; CC IsoId=P04233-1; Sequence=Displayed; CC Name=p35 {ECO:0000303|PubMed:3104027}; Synonyms=Short; CC IsoId=P04233-2; Sequence=VSP_005331; CC Name=3; CC IsoId=P04233-3; Sequence=VSP_037869, VSP_037870; CC Name=p41 {ECO:0000303|PubMed:3104027}; CC IsoId=P04233-4; Sequence=VSP_060904; CC Name=p33 {ECO:0000303|PubMed:3104027}; CC IsoId=P04233-5; Sequence=VSP_060904, VSP_005331; CC -!- TISSUE SPECIFICITY: Detected in urine (at protein level). CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313}. CC -!- TISSUE SPECIFICITY: [Isoform p41]: In B cells, represents 10% of total CC CD74 expression. {ECO:0000269|PubMed:3104027}. CC -!- TISSUE SPECIFICITY: [Isoform p33]: In B cells, represents 70% of total CC CD74 expression. {ECO:0000269|PubMed:3104027}. CC -!- DOMAIN: Antiviral activity requires delivery of the thyroglobulin CC domain to the endosomal membrane. {ECO:0000269|PubMed:32855215}. CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans CC (PubMed:22171320, PubMed:23234360). Contains chondroitin sulfate CC (PubMed:25326458). {ECO:0000269|PubMed:22171320, CC ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458}. CC -!- DISEASE: Note=A chromosomal aberration involving CD74 is found in a CC non-small cell lung tumor. Results in the formation of a CD74-ROS1 CC chimeric protein. {ECO:0000269|PubMed:12661006}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA36304.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; ALT_INIT; mRNA. DR EMBL; X00497; CAA25192.1; -; mRNA. DR EMBL; X00497; CAA25193.1; -; mRNA. DR EMBL; X03339; CAA27046.1; -; Genomic_DNA. DR EMBL; X03340; CAA27047.1; -; Genomic_DNA. 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; BT019505; AAV38312.1; -; mRNA. DR EMBL; AK292076; BAF84765.1; -; mRNA. DR EMBL; AK297889; BAG60210.1; -; mRNA. DR EMBL; AC011372; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011388; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61727.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61728.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61729.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61730.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61731.1; -; Genomic_DNA. DR EMBL; BC018726; AAH18726.1; -; mRNA. DR EMBL; BC024272; AAH24272.1; -; mRNA. DR CCDS; CCDS34276.1; -. [P04233-3] DR CCDS; CCDS47308.1; -. [P04233-2] DR CCDS; CCDS47309.1; -. [P04233-1] DR PIR; A93981; HLHUG. DR RefSeq; NP_001020329.1; NM_001025158.2. [P04233-3] DR RefSeq; NP_001020330.1; NM_001025159.2. [P04233-1] DR RefSeq; NP_004346.1; NM_004355.3. [P04233-2] DR PDB; 1A6A; X-ray; 2.75 A; C=103-117. DR PDB; 1ICF; X-ray; 2.00 A; I/J=210-274. DR PDB; 1IIE; NMR; -; A/B/C=134-208. DR PDB; 1L3H; NMR; -; A=210-274. DR PDB; 1MUJ; X-ray; 2.15 A; C=97-121. DR PDB; 3PDO; X-ray; 1.95 A; C=102-120. DR PDB; 3PGC; X-ray; 2.66 A; C/F=106-120. DR PDB; 3PGD; X-ray; 2.72 A; C/F=106-120. DR PDB; 3QXA; X-ray; 2.71 A; C/F=103-117. DR PDB; 3QXD; X-ray; 2.30 A; C/F=103-117. DR PDB; 4AEN; X-ray; 2.20 A; C=106-120. DR PDB; 4AH2; X-ray; 2.36 A; B=106-120. DR PDB; 4X5W; X-ray; 1.34 A; C=102-120. DR PDB; 5KSU; X-ray; 2.73 A; C/F=103-117. DR PDB; 5KSV; X-ray; 2.19 A; C=109-123. DR PDBsum; 1A6A; -. DR PDBsum; 1ICF; -. DR PDBsum; 1IIE; -. DR PDBsum; 1L3H; -. DR PDBsum; 1MUJ; -. DR PDBsum; 3PDO; -. DR PDBsum; 3PGC; -. DR PDBsum; 3PGD; -. DR PDBsum; 3QXA; -. DR PDBsum; 3QXD; -. DR PDBsum; 4AEN; -. DR PDBsum; 4AH2; -. DR PDBsum; 4X5W; -. DR PDBsum; 5KSU; -. DR PDBsum; 5KSV; -. DR AlphaFoldDB; P04233; -. DR BMRB; P04233; -. DR SMR; P04233; -. DR BioGRID; 107410; 143. DR ELM; P04233; -. DR IntAct; P04233; 200. DR MINT; P04233; -. DR STRING; 9606.ENSP00000009530; -. DR BindingDB; P04233; -. DR ChEMBL; CHEMBL4692; -. DR GuidetoPHARMACOLOGY; 2840; -. DR MEROPS; I31.002; -. DR TCDB; 9.A.75.1.1; the mhc ii receptor (mhc2r) family. DR GlyConnect; 659; 11 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site). DR GlyCosmos; P04233; 8 sites, 14 glycans. DR GlyGen; P04233; 12 sites, 11 N-linked glycans (2 sites), 4 O-linked glycans (7 sites). DR iPTMnet; P04233; -. DR PhosphoSitePlus; P04233; -. DR SwissPalm; P04233; -. DR BioMuta; CD74; -. DR DMDM; 20178292; -. DR CPTAC; CPTAC-5941; -. DR EPD; P04233; -. DR jPOST; P04233; -. DR MassIVE; P04233; -. DR MaxQB; P04233; -. DR PaxDb; P04233; -. DR PeptideAtlas; P04233; -. DR ProteomicsDB; 51689; -. [P04233-1] DR ProteomicsDB; 51690; -. [P04233-2] DR ProteomicsDB; 51691; -. [P04233-3] DR ABCD; P04233; 19 sequenced antibodies. DR Antibodypedia; 2245; 2434 antibodies from 53 providers. DR CPTC; P04233; 1 antibody. DR DNASU; 972; -. DR Ensembl; ENST00000009530.13; ENSP00000009530.7; ENSG00000019582.17. [P04233-1] DR Ensembl; ENST00000353334.11; ENSP00000230685.6; ENSG00000019582.17. [P04233-2] DR Ensembl; ENST00000377795.7; ENSP00000367026.3; ENSG00000019582.17. [P04233-3] DR GeneID; 972; -. DR KEGG; hsa:972; -. DR MANE-Select; ENST00000009530.13; ENSP00000009530.7; NM_001025159.3; NP_001020330.1. DR UCSC; uc003lsc.4; human. [P04233-1] DR AGR; HGNC:1697; -. DR CTD; 972; -. DR DisGeNET; 972; -. DR GeneCards; CD74; -. DR HGNC; HGNC:1697; CD74. DR HPA; ENSG00000019582; Tissue enhanced (lymphoid). DR MIM; 142790; gene. DR neXtProt; NX_P04233; -. DR OpenTargets; ENSG00000019582; -. DR PharmGKB; PA26236; -. DR VEuPathDB; HostDB:ENSG00000019582; -. DR eggNOG; KOG1214; Eukaryota. DR GeneTree; ENSGT00390000008961; -. DR InParanoid; P04233; -. DR OMA; HHNCSEP; -. DR OrthoDB; 2972165at2759; -. DR PhylomeDB; P04233; -. DR TreeFam; TF317779; -. DR PathwayCommons; P04233; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR SignaLink; P04233; -. DR SIGNOR; P04233; -. DR BioGRID-ORCS; 972; 13 hits in 1159 CRISPR screens. DR ChiTaRS; CD74; human. DR EvolutionaryTrace; P04233; -. DR GeneWiki; CD74; -. DR GenomeRNAi; 972; -. DR Pharos; P04233; Tchem. DR PRO; PR:P04233; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P04233; protein. DR Bgee; ENSG00000019582; Expressed in monocyte and 200 other tissues. DR ExpressionAtlas; P04233; baseline and differential. DR Genevisible; P04233; HS. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005770; C:late endosome; ISS:UniProtKB. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0005764; C:lysosome; ISS:UniProtKB. DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0042613; C:MHC class II protein complex; ISS:BHF-UCL. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0035693; C:NOS2-CD74 complex; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0005773; C:vacuole; IDA:BHF-UCL. DR GO; GO:0001540; F:amyloid-beta binding; IPI:BHF-UCL. DR GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA. DR GO; GO:0019955; F:cytokine binding; IPI:BHF-UCL. DR GO; GO:0004896; F:cytokine receptor activity; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; TAS:UniProtKB. DR GO; GO:0035718; F:macrophage migration inhibitory factor binding; IPI:BHF-UCL. DR GO; GO:0042289; F:MHC class II protein binding; ISS:BHF-UCL. DR GO; GO:0042658; F:MHC class II protein binding, via antigen binding groove; IDA:UniProtKB. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB. DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl. DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB. DR GO; GO:0019882; P:antigen processing and presentation; IBA:GO_Central. DR GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; NAS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl. DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0035691; P:macrophage migration inhibitory factor signaling pathway; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL. DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA: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; IEA:Ensembl. DR GO; GO:0002792; P:negative regulation of peptide secretion; IDA:BHF-UCL. DR GO; GO:0045581; P:negative regulation of T cell differentiation; IEA:Ensembl. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB. DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl. DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:BHF-UCL. DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISS:BHF-UCL. DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:ARUK-UCL. 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; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:CAFA. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:ARUK-UCL. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:ARUK-UCL. DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:CAFA. DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:BHF-UCL. DR GO; GO:2000448; P:positive regulation of macrophage migration inhibitory factor signaling pathway; IMP:ARUK-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA. DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:CAFA. DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL. DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:ARUK-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA. DR GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl. DR GO; GO:0002830; P:positive regulation of type 2 immune response; IBA:GO_Central. DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:CAFA. DR GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0070206; P:protein trimerization; IEA:InterPro. DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB. DR GO; GO:0043030; P:regulation of macrophage activation; NAS:UniProtKB. 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 GO; GO:0045058; P:T cell selection; NAS:UniProtKB. 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. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative initiation; KW Alternative splicing; Cell membrane; Chaperone; Direct protein sequencing; 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..296 FT /note="HLA class II histocompatibility antigen gamma chain" FT /id="PRO_0000067954" FT PEPTIDE 97..120 FT /note="Class-II-associated invariant chain peptide" FT /evidence="ECO:0000269|PubMed:1448172" FT /id="PRO_0000448886" FT TOPO_DOM 1..46 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 47..72 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 73..296 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 210..271 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 225..226 FT /note="Required for interaction with CTSL" FT /evidence="ECO:0000305|PubMed:10022822, FT ECO:0000305|PubMed:32855215" FT REGION 263..296 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 208..209 FT /note="Breakpoint for translocation to form a CD74-ROS1 FT fusion protein" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04441" FT CARBOHYD 130 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 203 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:22171320, FT ECO:0000269|PubMed:23234360" FT CARBOHYD 256 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10022822" FT CARBOHYD 281 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:23234360" FT CARBOHYD 282 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313" FT DISULFID 213..232 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:10022822" FT DISULFID 243..250 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:10022822" FT DISULFID 252..271 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:10022822" FT VAR_SEQ 1..16 FT /note="Missing (in isoform p41 and isoform p33)" FT /evidence="ECO:0000303|PubMed:3104027" FT /id="VSP_060904" FT VAR_SEQ 148..160 FT /note="NADPLKVYPPLKG -> SHWNWRTRLLGWV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037869" FT VAR_SEQ 161..296 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037870" FT VAR_SEQ 209..272 FT /note="Missing (in isoform p35 and isoform p33)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:6324166, FT ECO:0000303|PubMed:6586420, ECO:0000303|Ref.5" FT /id="VSP_005331" FT MUTAGEN 225..226 FT /note="PG->RR,DD: Decreases inhibition of Ebola virus FT infection." FT /evidence="ECO:0000269|PubMed:32855215" FT MUTAGEN 225..226 FT /note="PG->TT: No effect on inhibition of Ebola virus FT infection." FT /evidence="ECO:0000269|PubMed:32855215" FT CONFLICT 167 FT /note="R -> T (in Ref. 3; CAA27047)" FT /evidence="ECO:0000305" FT HELIX 139..149 FT /evidence="ECO:0007829|PDB:1IIE" FT HELIX 162..172 FT /evidence="ECO:0007829|PDB:1IIE" FT HELIX 175..194 FT /evidence="ECO:0007829|PDB:1IIE" FT HELIX 212..217 FT /evidence="ECO:0007829|PDB:1ICF" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:1L3H" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:1ICF" FT TURN 245..248 FT /evidence="ECO:0007829|PDB:1ICF" FT STRAND 249..253 FT /evidence="ECO:0007829|PDB:1ICF" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:1ICF" 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 //