ID   TIMD2_RAT               Reviewed;         349 AA.
AC   Q5FVR0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=T-cell immunoglobulin and mucin domain-containing protein 2;
DE            Short=TIMD-2;
DE   AltName: Full=T-cell immunoglobulin mucin receptor 2;
DE            Short=TIM-2;
DE   AltName: Full=T-cell membrane protein 2;
DE   Flags: Precursor;
GN   Name=Timd2; Synonyms=Tim2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
CC   -!- FUNCTION: Probable receptor for SEMA4A involved in the regulation of T-
CC       cell function. The interaction with SEMA4A enhances T-cell activation
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Human appears to lack the Timd2 gene.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.
CC       {ECO:0000305}.
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DR   EMBL; BC089832; AAH89832.1; -; mRNA.
DR   RefSeq; NP_001013877.1; NM_001013855.1.
DR   RefSeq; XP_006246230.1; XM_006246168.2.
DR   RefSeq; XP_008765891.1; XM_008767669.2.
DR   AlphaFoldDB; Q5FVR0; -.
DR   SMR; Q5FVR0; -.
DR   STRING; 10116.ENSRNOP00000056223; -.
DR   GlyGen; Q5FVR0; 2 sites.
DR   PaxDb; Q5FVR0; -.
DR   PRIDE; Q5FVR0; -.
DR   Ensembl; ENSRNOT00000059468; ENSRNOP00000056223; ENSRNOG00000021345.
DR   GeneID; 287222; -.
DR   KEGG; rno:287222; -.
DR   UCSC; RGD:1359571; rat.
DR   CTD; 171284; -.
DR   RGD; 1359571; Timd2.
DR   eggNOG; ENOG502S454; Eukaryota.
DR   GeneTree; ENSGT00940000159345; -.
DR   HOGENOM; CLU_047504_2_1_1; -.
DR   InParanoid; Q5FVR0; -.
DR   OMA; CRYNGAI; -.
DR   OrthoDB; 1147868at2759; -.
DR   PhylomeDB; Q5FVR0; -.
DR   TreeFam; TF336163; -.
DR   PRO; PR:Q5FVR0; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000021345; Expressed in liver and 10 other tissues.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070287; F:ferritin receptor activity; ISO:RGD.
DR   GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR   GO; GO:0001618; F:virus receptor activity; IBA:GO_Central.
DR   GO; GO:0006826; P:iron ion transport; ISO:RGD.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR   GO; GO:0033005; P:positive regulation of mast cell activation; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..349
FT                   /note="T-cell immunoglobulin and mucin domain-containing
FT                   protein 2"
FT                   /id="PRO_0000042100"
FT   TOPO_DOM        21..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..123
FT                   /note="Ig-like V-type"
FT   REGION          128..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        48..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        54..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   349 AA;  38544 MW;  69FFF53E9C581416 CRC64;
     MVQLQVFISG LLLLLPGAVA SYTVVQGHSV TLPCIYSTTY RDEMVPTCWG RGECRSSYCT
     RSLIWTNGYK VTYQRSNRYQ LKGNISEGNV SLTIENTVVS DSGPYCCIAE IPGAFYFVDY
     LLEVKAELPT SPPTRPTNTG RPTTTRPTNT GRPTTTRPTN TGRPTTTERP TTTGRPTTTE
     RPTTTGRPTT ISTRSTHVPT STRVSTSTPP TPEQTQTHRS EATTYYPDQT TAEVTEAPSH
     TPTDWNNTAT SSDDSWNSDT EAIPPQKLQR NPTKGFYVGM SFAALLLLLL ASTVAITRYM
     VMRKNSGSLR FVAFPVSKIG ASQNKVVEQA RIEDEVYIIE DSPYFEEES