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NILR1_RAT
ID   NILR1_RAT               Reviewed;         547 AA.
AC   D3ZQX2; A2J8C0;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 3.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Neutrophil immunoglobulin-like receptor 1 {ECO:0000303|PubMed:10382763};
DE   Flags: Precursor;
GN   Name=Nilr1 {ECO:0000303|PubMed:10382763};
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:0000312|Proteomes:UP000002494};
RN   [1] {ECO:0000312|EMBL:AAD29110.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=PVG {ECO:0000312|EMBL:AAD29110.1};
RC   TISSUE=Natural killer cell {ECO:0000303|PubMed:10382763};
RX   PubMed=10382763;
RX   DOI=10.1002/(sici)1521-4141(199906)29:06<2000::aid-immu2000>3.0.co;2-5;
RA   Berg S.F., Fossum S., Dissen E.;
RT   "NILR-1, a novel immunoglobulin-like receptor expressed by neutrophilic
RT   granulocytes, is encoded by a leukocyte receptor gene complex on rat
RT   chromosome 1.";
RL   Eur. J. Immunol. 29:2000-2006(1999).
RN   [2] {ECO:0000312|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
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   [3] {ECO:0000312|EMBL:EDL84917.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expression detected in neutrophilic granulocytes.
CC       {ECO:0000269|PubMed:10382763}.
CC   -!- DOMAIN: Contains 4 copies of a cytoplasmic motif that is referred to as
CC       the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC       involved in modulation of cellular responses. The phosphorylated ITIM
CC       motif can bind the SH2 domain of several SH2-containing phosphatases.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDL84917.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF082534; AAD29110.1; -; mRNA.
DR   EMBL; AABR07071875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474101; EDL84917.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_113901.2; NM_031713.1.
DR   AlphaFoldDB; D3ZQX2; -.
DR   SMR; D3ZQX2; -.
DR   STRING; 10116.ENSRNOP00000015054; -.
DR   GlyGen; D3ZQX2; 2 sites.
DR   PaxDb; D3ZQX2; -.
DR   Ensembl; ENSRNOT00000084439; ENSRNOP00000075718; ENSRNOG00000054954.
DR   GeneID; 65146; -.
DR   KEGG; rno:65146; -.
DR   UCSC; RGD:70895; rat.
DR   CTD; 10288; -.
DR   RGD; 70895; Nilr1.
DR   eggNOG; ENOG502RYEX; Eukaryota.
DR   GeneTree; ENSGT01000000214458; -.
DR   HOGENOM; CLU_021100_2_3_1; -.
DR   InParanoid; D3ZQX2; -.
DR   OrthoDB; 1000446at2759; -.
DR   PhylomeDB; D3ZQX2; -.
DR   TreeFam; TF336644; -.
DR   PRO; PR:D3ZQX2; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Proteomes; UP000234681; Chromosome 1.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR   GO; GO:0032396; F:inhibitory MHC class I receptor activity; ISO:RGD.
DR   GO; GO:0042288; F:MHC class I protein binding; ISO:RGD.
DR   GO; GO:0023029; F:MHC class Ib protein binding; ISO:RGD.
DR   GO; GO:0023025; F:MHC class Ib protein complex binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; ISO:RGD.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR   GO; GO:0002767; P:immune response-inhibiting cell surface receptor signaling pathway; ISO:RGD.
DR   GO; GO:0140105; P:interleukin-10-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0002578; P:negative regulation of antigen processing and presentation; ISO:RGD.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:RGD.
DR   GO; GO:2000524; P:negative regulation of T cell costimulation; ISO:RGD.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0002666; P:positive regulation of T cell tolerance induction; ISO:RGD.
DR   GO; GO:0002645; P:positive regulation of tolerance induction; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   Gene3D; 2.60.40.10; -; 3.
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   Pfam; PF13895; Ig_2; 1.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..547
FT                   /note="Neutrophil immunoglobulin-like receptor 1"
FT                   /id="PRO_0000435369"
FT   TOPO_DOM        24..345
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..547
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          34..119
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          132..222
FT                   /note="Ig-like C2-type 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          233..321
FT                   /note="Ig-like C2-type 3"
FT                   /evidence="ECO:0000255"
FT   REGION          377..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           417..422
FT                   /note="ITIM motif 1"
FT                   /evidence="ECO:0000303|PubMed:10382763"
FT   MOTIF           446..451
FT                   /note="ITIM motif 2"
FT                   /evidence="ECO:0000303|PubMed:10382763"
FT   MOTIF           498..503
FT                   /note="ITIM motif 3"
FT                   /evidence="ECO:0000303|PubMed:10382763"
FT   MOTIF           528..533
FT                   /note="ITIM motif 4"
FT                   /evidence="ECO:0000303|PubMed:10382763"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..99
FT                   /evidence="ECO:0000305"
FT   DISULFID        147..199
FT                   /evidence="ECO:0000305"
FT   DISULFID        248..299
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  61258 MW;  44EBCAC3304D9A0C CRC64;
     MTFTCKALLC LGMTLGLWIT VLTEFLPRPI LRVQPDTVVS TQSKVIFFCE RSQGAELYCL
     YKKGNPRNPR CKEIRPKPGK KVEFFISKIE PYHAGHYHCY YQIHGQWSED SDALELVVTG
     VYDYNELRLS VLPSPVVTVG RNMTLHCISH SHYDKFILTK EDHKFTSSLD TQCIPPSGQC
     QALFVMGPMT SNHTGTFRCY GYYKHTPQLW SIPSEPLEIH ISGLSKKPSL LTHQGHILDP
     GVNLTLQCCS DINYDRFALY KVGGVDIMQH TSQQTDTGFS MTNFTLGYVH HSTGGQYRCY
     GAHNLSSEWS ASSDPLDILI TGPIQMSTLP PITSMPPDQL ESYVNALIGV SVAFLVFLFI
     LIFIILQRRH QRKFRKDGEE AQKEKELQYP TGAVEPISRD RDQQKRSNAA AATQEESVYA
     SVEDMETEDG VELDTWKPPE GDPQGETYAQ VKPSRLRRVE AIIPSAMSRE QLNTKYEQAE
     EGQEVDGQAT ESEEPQDVTY AQLCSRTLRQ GTAAPPLSQA GEAPEEPSVY AALATACPGA
     VPKDKEQ
 
 
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