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Database: UniProt
Entry: M0R692_RAT
LinkDB: M0R692_RAT
Original site: M0R692_RAT 
ID   M0R692_RAT              Unreviewed;       105 AA.
AC   M0R692;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
GN   Name=ENSRNOG00000069250 {ECO:0000313|RGD:150343150};
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 {ECO:0000313|Ensembl:ENSRNOP00000064935.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000064935.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000064935.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000064935.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000064935.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; M0R692; -.
DR   STRING; 10116.ENSRNOP00000064935; -.
DR   PaxDb; 10116-ENSRNOP00000064935; -.
DR   PeptideAtlas; M0R692; -.
DR   Ensembl; ENSRNOT00000073713.2; ENSRNOP00000064935.2; ENSRNOG00000069250.1.
DR   AGR; RGD:150343150; -.
DR   RGD; 150343150; ENSRNOG00000069250.
DR   VEuPathDB; HostDB:ENSRNOG00000069250; -.
DR   eggNOG; ENOG502SQT3; Eukaryota.
DR   GeneTree; ENSGT00950000183013; -.
DR   HOGENOM; CLU_077975_5_2_1; -.
DR   InParanoid; M0R692; -.
DR   OMA; MRWITLY; -.
DR   Reactome; R-RNO-166663; Initial triggering of complement.
DR   Reactome; R-RNO-173623; Classical antibody-mediated complement activation.
DR   Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-RNO-2029481; FCGR activation.
DR   Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR   Reactome; R-RNO-2454202; Fc epsilon receptor (FCERI) signaling.
DR   Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-RNO-5690714; CD22 mediated BCR regulation.
DR   Reactome; R-RNO-977606; Regulation of Complement cascade.
DR   Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000050652; Expressed in jejunum and 8 other cell types or tissues.
DR   GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR23266; IMMUNOGLOBULIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR23266:SF381; IMMUNOGLOBULIN HEAVY VARIABLE 1-82; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   4: Predicted;
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Immunoglobulin {ECO:0000256|ARBA:ARBA00043265};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          1..105
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   105 AA;  11301 MW;  709547AE027D69AC CRC64;
     QVKLLQSGAE LVKPGASVKL SCKTSGFTFS TSYMSWLKQV PGPSIEWIGW IYAGDGGTNY
     NQKFKGKATL TVDKSSSTAY MDLSSLTSED AAVYFCARHS VVTTS
//
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