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Database: UniProt
Entry: S7N2W2_MYOBR
LinkDB: S7N2W2_MYOBR
Original site: S7N2W2_MYOBR 
ID   S7N2W2_MYOBR            Unreviewed;       295 AA.
AC   S7N2W2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=HLA class II histocompatibility antigen gamma chain {ECO:0000313|EMBL:EPQ10330.1};
GN   ORFNames=D623_10034754 {ECO:0000313|EMBL:EPQ10330.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ10330.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR   EMBL; KE162980; EPQ10330.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7N2W2; -.
DR   MEROPS; I31.002; -.
DR   eggNOG; KOG1214; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035718; F:macrophage migration inhibitory factor binding; IEA:InterPro.
DR   GO; GO:0042289; F:MHC class II protein binding; IEA:InterPro.
DR   GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0070206; P:protein trimerization; IEA:InterPro.
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   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR001992-1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          179..240
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REGION          271..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        182..201
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001992-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        212..219
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001992-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        221..240
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001992-1"
SQ   SEQUENCE   295 AA;  33193 MW;  B63554CAD41354D2 CRC64;
     MLGQRPGAQE SKCSRGALYT GFSVLVALLL AGQATTAYFL YQQQGRLDKL TVTSQNLQLE
     NLRMKLPKSA KPVGKMRVAT PMLMQALPME GLLQGPMQNA TKYGNTTMDH VMHLLLKADP
     LKVYPQMKGS FPENLKHLKK TMEGLDWKIF ESWMHQWLLF EMSKNSLGEK LTEGSPKVLT
     KCLEEASRIP AIHPGRFKPQ CDENGNYMPL QCFGSIGYCW CVFPNGTEVP HTRSRGRHNC
     SEPLDMEDLS SGLGVTKQDL VQEITSEQQI RRALLPKPPS ISRHTRPKEL DHELG
//
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