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Database: UniProt
Entry: D3ZF71_RAT
LinkDB: D3ZF71_RAT
Original site: D3ZF71_RAT 
ID   D3ZF71_RAT              Unreviewed;       372 AA.
AC   D3ZF71;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Sialic acid binding Ig-like lectin 10 {ECO:0000313|Ensembl:ENSRNOP00000015941.4};
GN   Name=Siglec10 {ECO:0000313|Ensembl:ENSRNOP00000015941.4,
GN   ECO:0000313|RGD:1307441};
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:ENSRNOP00000015941.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000015941.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000015941.4,
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:ENSRNOP00000015941.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000015941.4};
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; NP_001099720.1; NM_001106250.1.
DR   AlphaFoldDB; D3ZF71; -.
DR   SMR; D3ZF71; -.
DR   PaxDb; 10116-ENSRNOP00000015941; -.
DR   Ensembl; ENSRNOT00000015941.6; ENSRNOP00000015941.4; ENSRNOG00000037339.5.
DR   KEGG; rno:292844; -.
DR   UCSC; RGD:1307441; rat.
DR   AGR; RGD:1307441; -.
DR   CTD; 89790; -.
DR   RGD; 1307441; Siglec10.
DR   eggNOG; ENOG502S41V; Eukaryota.
DR   GeneTree; ENSGT01080000257333; -.
DR   HOGENOM; CLU_024444_6_2_1; -.
DR   OrthoDB; 2963061at2759; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000037339; Expressed in spleen and 6 other cell types or tissues.
DR   ExpressionAtlas; D3ZF71; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0019902; F:phosphatase binding; ISO:RGD.
DR   GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR   GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0106015; P:negative regulation of inflammatory response to wounding; ISO:RGD.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR   PANTHER; PTHR12035:SF115; SIALIC ACID-BINDING IG-LIKE LECTIN 10; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   372 AA;  40758 MW;  FCA824E9D703F859 CRC64;
     MLCPGRRPWP AWSQFPVFIA DPPEDLRVTV SQENRTVLEI LRNGTSLPVL EGQSLCLVCV
     TYSNPPASVS WFGATQTLIP TQSSEPGVLE LPLVQREHEG ELTCAAQSPL GTQRISLSLS
     VHYPPQMSRP SCSWDSEGLH CSCSSRAWPA PSLRWRLGEG LLEGNSSNAS FKVTSSSLGP
     WANSSLSLLQ ELEPSLWLSC EAWNTHGAQT TSVLLLPDKN SSAAFSKGAA LGFGITALLA
     LCLVVIIMKT LQKKGTQEVT SRPKISRGST ILDYINVVPK TRSPARNWKA EPDTPSGISP
     LDTHSPKPKK KQKDPRFTSP GFPDPRPSSQ APVSENNPEE LHYAALNFPR LRLRETQNPQ
     DTYSDYAEVR VH
//
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