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 24-JAN-2024, entry version 91. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000075718; -. DR GlyCosmos; D3ZQX2; 2 sites, No reported glycans. DR GlyGen; D3ZQX2; 2 sites. DR PhosphoSitePlus; D3ZQX2; -. DR PaxDb; 10116-ENSRNOP00000015054; -. DR Ensembl; ENSRNOT00000084439.2; ENSRNOP00000075718.2; ENSRNOG00000054954.2. DR Ensembl; ENSRNOT00060050036; ENSRNOP00060041704; ENSRNOG00060028731. DR GeneID; 65146; -. DR KEGG; rno:65146; -. DR UCSC; RGD:70895; rat. DR AGR; RGD:70895; -. DR CTD; 10288; -. DR RGD; 70895; Nilr1. DR eggNOG; ENOG502RYEX; Eukaryota. DR GeneTree; ENSGT01100000263478; -. DR HOGENOM; CLU_021100_2_3_1; -. DR InParanoid; D3ZQX2; -. DR OMA; THITEHD; -. DR OrthoDB; 5353978at2759; -. DR PhylomeDB; D3ZQX2; -. DR TreeFam; TF336644; -. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR PRO; PR:D3ZQX2; -. DR Proteomes; UP000002494; Chromosome 1. DR Proteomes; UP000234681; Chromosome 1. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0032396; F:inhibitory MHC class I receptor activity; IBA:GO_Central. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR PANTHER; PTHR11738:SF179; LEUKOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR SUBFAMILY A MEMBER 5; 1. DR PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1. DR Pfam; PF13895; Ig_2; 1. DR SMART; SM00409; IG; 3. DR SUPFAM; SSF48726; Immunoglobulin; 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 //