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Database: UniProt
Entry: G1SNV3_RABIT
LinkDB: G1SNV3_RABIT
Original site: G1SNV3_RABIT 
ID   G1SNV3_RABIT            Unreviewed;       560 AA.
AC   G1SNV3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004690.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000004690.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000004690.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004690.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC       acid binding Ig-like lectin) family. {ECO:0000256|ARBA:ARBA00038361}.
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DR   RefSeq; XP_002722392.2; XM_002722346.3.
DR   AlphaFoldDB; G1SNV3; -.
DR   Ensembl; ENSOCUT00000005407.4; ENSOCUP00000004690.3; ENSOCUG00000005408.4.
DR   GeneID; 100351300; -.
DR   KEGG; ocu:100351300; -.
DR   CTD; 8778; -.
DR   eggNOG; ENOG502S41V; Eukaryota.
DR   GeneTree; ENSGT01080000257333; -.
DR   HOGENOM; CLU_024444_6_1_1; -.
DR   OrthoDB; 5350608at2759; -.
DR   TreeFam; TF332441; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000005408; Expressed in blood and 18 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR   PANTHER; PTHR12035:SF103; SIALIC ACID-BINDING IG-LIKE LECTIN 5; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..560
FT                   /note="Ig-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023806401"
FT   TRANSMEM        448..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..130
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          147..230
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          252..334
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          477..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  60810 MW;  EB44D8EE13376A10 CRC64;
     MLPLLLLLPL LWGGSLQEAP GYELQVQRSV TVQEGLCVSV PCSFSYPTSY WGSSSQVYIF
     WFREGDHIYY DAPVATNHPQ RPVKTEAQGR FHVSSDLWTP NCSLSIRDAR WGDTGWYFFR
     VETGRDVKYN YVETKLYLHV TALTEKPHVH VPASLESGCP TQLTCSLPGS CPGGRPLSFS
     WAGEALGSRD PRTLRSPLLT FTPRPQDHDT SLTCRVNLQG ARVTTERTVQ LNVSYAVQNL
     TVRAFLGNST GSQILKSGST FSIMEGLALR LLCQVDSNSC ANLSWFQGSP AENAIPISTN
     NSLELPQVQP EHEGVFTCLA QNPLGSLQGS VNLSVYYPAQ LFGPSCSWEA GGLHCSCSSR
     ARPAPSLRWR LGERLLAGNS SGNSSHASFT VTSSSAGPWA NSSLSLHGEL GSDLRLSCEA
     WNVHRTHNVT FLLLPGKAAW EGGVVSTALA GAGAIALLGL CLCLLVLGIV KICRKPAAGR
     PEGAEDEDPV MGSVTWDSRQ KAPKPDGPQE QDSPADAAPL PQQPQELHYA SLSFHGMKPR
     EPQEQEATRA TEYSEIKKSK
//
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