LRB3L_RAT
ID LRB3L_RAT Reviewed; 761 AA.
AC A0A0G2KBC9; A2JHX5; A2JHX6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 3-like {ECO:0000312|RGD:1307219};
DE Flags: Precursor;
GN Name=Lilrb3l {ECO:0000312|RGD:1307219};
GN Synonyms=Pir-A1 {ECO:0000303|PubMed:10586026},
GN Pirb {ECO:0000303|PubMed:10586026};
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:AAD50899.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=Lewis {ECO:0000312|EMBL:AAD50899.1};
RC TISSUE=Spleen {ECO:0000303|PubMed:10586026};
RX PubMed=10586026;
RA Dennis G. Jr., Stephan R.P., Kubagawa H., Cooper M.D.;
RT "Characterization of paired Ig-like receptors in rats.";
RL J. Immunol. 163:6371-6377(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).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A0G2KBC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A0G2KBC9-2; Sequence=VSP_058098, VSP_058099, VSP_058100;
CC -!- TISSUE SPECIFICITY: Detected in spleen, bone marrow, thymus, ovary and
CC lung. {ECO:0000269|PubMed:10586026}.
CC -!- DOMAIN: Contains 3 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 including PTPN6/SHP-1, resulting in the dephosphorylation of the
CC downstream protein kinases SYK and BTK. {ECO:0000250|UniProtKB:P97484}.
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DR EMBL; AF169636; AAD50899.1; -; mRNA.
DR EMBL; AF169637; AAD50905.1; -; mRNA.
DR EMBL; AABR07001996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07001997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07001998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07001999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07071875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0G2KBC9; -.
DR SMR; A0A0G2KBC9; -.
DR GlyGen; A0A0G2KBC9; 5 sites.
DR RGD; 1307219; Lilrb3l.
DR VEuPathDB; HostDB:ENSRNOG00000058422; -.
DR PhylomeDB; A0A0G2KBC9; -.
DR PRO; PR:A0A0G2KBC9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000053260; Expressed in spleen and 20 other tissues.
DR ExpressionAtlas; A0A0G2KBC9; baseline and differential.
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: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; -; 6.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..761
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 3-like"
FT /evidence="ECO:0000255"
FT /id="PRO_5002547075"
FT TOPO_DOM 25..560
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..116
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 117..219
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 223..314
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 322..415
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 480..559
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT REGION 589..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 632..637
FT /note="ITIM motif 1"
FT /evidence="ECO:0000305"
FT MOTIF 712..717
FT /note="ITIM motif 2"
FT /evidence="ECO:0000305"
FT MOTIF 742..747
FT /note="ITIM motif 3"
FT /evidence="ECO:0000305"
FT COMPBIAS 706..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..97
FT /evidence="ECO:0000305"
FT DISULFID 143..196
FT /evidence="ECO:0000305"
FT DISULFID 245..294
FT /evidence="ECO:0000305"
FT DISULFID 341..393
FT /evidence="ECO:0000305"
FT DISULFID 498..549
FT /evidence="ECO:0000305"
FT VAR_SEQ 479
FT /note="T -> TLGYGRHSTGGKYRCYGAHNLSSEWSASSDPLDILITGQLDLAPS
FT (in isoform 2)"
FT /id="VSP_058098"
FT VAR_SEQ 560..634
FT /note="KALIGVSVAFLLFLFILIFILLRRRHQEKFRKDDEDAQKGKELQLSTGAAEP
FT VTRDRGHQKRSNPAAATQEESLY -> LSFASAPVELIVSESIEASSWPAKRFITTATP
FT ENQDHTTEFLIRMGMAVLVLIVLSILAAEPWQSHRQTHHAAGK (in isoform 2)"
FT /id="VSP_058099"
FT VAR_SEQ 635..761
FT /note="Missing (in isoform 2)"
FT /id="VSP_058100"
FT CONFLICT 93
FT /note="Q -> R (in Ref. 1; AAD50899/AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="G -> E (in Ref. 1; AAD50899/AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="T -> I (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="M -> L (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="T -> M (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="S -> P (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="L -> R (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="I -> F (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 537..538
FT /note="SG -> RA (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="H -> P (in Ref. 1; AAD50905)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="T -> K (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="A -> G (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 687..688
FT /note="NT -> KK (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 692..693
FT /note="QA -> KE (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="D -> E (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="T -> I (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="Q -> K (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="T -> K (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="N -> K (in Ref. 1; AAD50899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 84944 MW; D0FB3CBBA19DE1A8 CRC64;
MTFTFTALLC LGLTLRLWIP VLTGSLPKPI LRVQPDSVVS MGTKVTFVCE ETIGVKESHL
YRNGNLQRTV LKNHQKPTNK TEFSFSNVDQ QMQQYQCSYR TQTKSSDYSE PLELVVTGAY
SKPSLSAQTN PVVTSGGYVT LKCEPSQDNH TLILTVEGSQ KHSWRKDPEC NRYTEKCHAL
FYVGPLTSNQ RWIFRCYSYE KHTPQVWSAP SEPVELLVSG KLQKTTIKAE PGSVIRSGRA
MTIWCQGDLD AEIYFLHKEG SHNTQSTQTL QQPGNKAKFL IPSVTQRHAG QYRCYCYSSA
GWSEPSDTLE LVVTGIYYYG VKLSGLPSPV VPEGGNVTLH CTSHSNYDKF ILTKEDQKFT
SSLDAEYIPS TGQHQALFVM GPMTPNYSGT FRCYGYYKHT PQLWSVPSEL LKIFISGPSR
KPSLLSHQGH ILEPGMSLTL QCYSDTKYDK FALYKEGGTD IIESFSQWTK AGLSMTNFTL
SVMPNSTVHS GENVTLMCWS TYSVDTFILS KEGSGQPPLR LKSKIQDQQY QSEFSMSGVT
SKLSGTYRCY GSHDSSLYLK ALIGVSVAFL LFLFILIFIL LRRRHQEKFR KDDEDAQKGK
ELQLSTGAAE PVTRDRGHQK RSNPAAATQE ESLYASVEDM ETKDGVELDT WKPPEGDPQG
ETYAQVEPSR LRRAGAISPV VSREQLNTKY EQAEEGQEVD SQATESEEPQ DVTYAQLCSR
TLRQGTAAPP LSQAGEAPEE PSVYAALATA RPGAVPKNKK Q
