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Database: UniProt
Entry: A0A087XGP4_POEFO
LinkDB: A0A087XGP4_POEFO
Original site: A0A087XGP4_POEFO 
ID   A0A087XGP4_POEFO        Unreviewed;       285 AA.
AC   A0A087XGP4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=CD74 molecule {ECO:0000313|Ensembl:ENSPFOP00000004947.1};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000004947.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000004947.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; AYCK01002990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007548367.1; XM_007548305.2.
DR   AlphaFoldDB; A0A087XGP4; -.
DR   STRING; 48698.ENSPFOP00000004947; -.
DR   Ensembl; ENSPFOT00000004956.2; ENSPFOP00000004947.1; ENSPFOG00000004979.2.
DR   GeneID; 103135523; -.
DR   KEGG; pfor:103135523; -.
DR   CTD; 58113; -.
DR   eggNOG; KOG1214; Eukaryota.
DR   GeneTree; ENSGT00390000008961; -.
DR   OMA; HHNCSEP; -.
DR   OrthoDB; 2972165at2759; -.
DR   Proteomes; UP000028760; 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:UP000028760};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..257
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        200..218
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001992-1"
FT   DISULFID        229..236
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001992-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        238..257
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001992-1"
SQ   SEQUENCE   285 AA;  31687 MW;  81F121F6CE703ED9 CRC64;
     MADNQEDAPL ARGSVSGSHE VLVNNAGPRG GSNSRALKIA GLTTLACLLL ASQVFTAYMV
     FDQKQQIHTL KKSSERMSKQ VTRVSQGGVA PARMAMPMNS LPLLADFTED DTSSKTPLTK
     VEDIAIVSVE KQVMDMMKDV SLPQFNETFL ANLRSLQQQI NESEWKNFES WMRYWLIFQM
     AQQKPAGPTP QPASLIKTKC QMEATPGVGK IGAYKPQCDE QGHYKPMQCW HATGFCWCVD
     QSGNPIQGTT MRGRPDCNRG AGFRRMMVAP RMMQKTFLEE EGKVN
//
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