ID SIGL5_HUMAN Reviewed; 551 AA. AC O15389; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-FEB-2019, entry version 163. DE RecName: Full=Sialic acid-binding Ig-like lectin 5; DE Short=Siglec-5; DE AltName: Full=CD33 antigen-like 2; DE AltName: Full=Obesity-binding protein 2; DE Short=OB-BP2; DE Short=OB-binding protein 2; DE AltName: CD_antigen=CD170; DE Flags: Precursor; GN Name=SIGLEC5; Synonyms=CD33L2, OBBP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TRP-358. RC TISSUE=Macrophage; RX PubMed=9731071; RA Cornish A.L., Freeman S., Forbes G., Ni J., Zhang M., Cepeda M., RA Gentz R., Augustus M., Carter K.C., Crocker P.R.; RT "Characterization of siglec-5, a novel glycoprotein expressed on RT myeloid cells related to CD33."; RL Blood 92:2123-2132(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Erythroleukemia; RX PubMed=10428856; DOI=10.1074/jbc.274.32.22729; RA Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C., RA Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F., RA Varki A., Kastelein R.A.; RT "OB-BP1/Siglec-6. A leptin- and sialic acid-binding protein of the RT immunoglobulin superfamily."; RL J. Biol. Chem. 274:22729-22738(1999). RN [3] RP ERRATUM. RA Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C., RA Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F., RA Varki A., Kastelein R.A.; RL J. Biol. Chem. 274:28058-28058(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-499. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-233 ALONE AND IN COMPLEX RP WITH ALPHA-LINKED SIALYLLACTOSES, DISULFIDE BONDS, AND SIALIC ACID RP BINDING SITES. RX PubMed=18022638; DOI=10.1016/j.jmb.2007.10.009; RA Zhuravleva M.A., Trandem K., Sun P.D.; RT "Structural implications of Siglec-5-mediated sialoglycan RT recognition."; RL J. Mol. Biol. 375:437-447(2008). CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid CC dependent binding to cells. Binds equally to alpha-2,3-linked and CC alpha-2,6-linked sialic acid. The sialic acid recognition site may CC be masked by cis interactions with sialic acids on the same cell CC surface. CC -!- INTERACTION: CC O00206:TLR4; NbExp=2; IntAct=EBI-750381, EBI-528701; CC Q15645:TRIP13; NbExp=4; IntAct=EBI-750381, EBI-358993; CC Q08AM6:VAC14; NbExp=5; IntAct=EBI-750381, EBI-2107455; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed by monocytic/myeloid lineage cells. CC Found at high levels in peripheral blood leukocytes, spleen, bone CC marrow and at lower levels in lymph node, lung, appendix, CC placenta, pancreas and thymus. Expressed by monocytes and CC neutrophils but absent from leukemic cell lines representing early CC stages of myelomonocytic differentiation. CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to CC as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This CC motif is involved in modulation of cellular responses. The CC phosphorylated ITIM motif can bind the SH2 domain of several SH2- CC containing phosphatases. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC CC (sialic acid binding Ig-like lectin) family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Siglec-5; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_272"; 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; AF170484; AAD50978.1; -; mRNA. DR EMBL; U71383; AAB70703.1; -; mRNA. DR EMBL; AC018755; AAF87846.1; -; Genomic_DNA. DR EMBL; BC029896; AAH29896.1; -; mRNA. DR CCDS; CCDS33088.1; -. DR RefSeq; NP_003821.1; NM_003830.3. DR UniGene; Hs.310333; -. DR PDB; 2ZG1; X-ray; 2.70 A; A=20-233. DR PDB; 2ZG2; X-ray; 2.85 A; A=20-233. DR PDB; 2ZG3; X-ray; 3.00 A; A=20-233. DR PDBsum; 2ZG1; -. DR PDBsum; 2ZG2; -. DR PDBsum; 2ZG3; -. DR ProteinModelPortal; O15389; -. DR SMR; O15389; -. DR BioGrid; 114308; 12. DR IntAct; O15389; 16. DR STRING; 9606.ENSP00000455510; -. DR UniLectin; O15389; -. DR iPTMnet; O15389; -. DR PhosphoSitePlus; O15389; -. DR BioMuta; SIGLEC5; -. DR EPD; O15389; -. DR PaxDb; O15389; -. DR PeptideAtlas; O15389; -. DR PRIDE; O15389; -. DR ProteomicsDB; 48625; -. DR DNASU; 8778; -. DR Ensembl; ENST00000534261; ENSP00000473238; ENSG00000105501. DR GeneID; 8778; -. DR KEGG; hsa:8778; -. DR UCSC; uc002pxe.5; human. DR CTD; 8778; -. DR DisGeNET; 8778; -. DR EuPathDB; HostDB:ENSG00000105501.11; -. DR GeneCards; SIGLEC5; -. DR HGNC; HGNC:10874; SIGLEC5. DR HPA; CAB024900; -. DR HPA; HPA009085; -. DR MIM; 604200; gene. DR neXtProt; NX_O15389; -. DR OpenTargets; ENSG00000105501; -. DR OpenTargets; ENSG00000268500; -. DR PharmGKB; PA35775; -. DR eggNOG; ENOG410IJT6; Eukaryota. DR eggNOG; ENOG410YKZU; LUCA. DR GeneTree; ENSGT00940000153211; -. DR HOGENOM; HOG000236324; -. DR HOVERGEN; HBG036161; -. DR InParanoid; O15389; -. DR KO; K06549; -. DR OMA; CSCSFRA; -. DR OrthoDB; 873673at2759; -. DR PhylomeDB; O15389; -. DR TreeFam; TF332441; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; SIGLEC5; human. DR EvolutionaryTrace; O15389; -. DR GeneWiki; SIGLEC5; -. DR GenomeRNAi; 8778; -. DR PRO; PR:O15389; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000105501; Expressed in 80 organ(s), highest expression level in blood. DR Genevisible; O15389; HS. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 4. 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 Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 1. DR SUPFAM; SSF48726; SSF48726; 4. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Complete proteome; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Lectin; Membrane; Polymorphism; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 16 {ECO:0000255}. FT CHAIN 17 551 Sialic acid-binding Ig-like lectin 5. FT /FTId=PRO_0000014944. FT TOPO_DOM 17 441 Extracellular. {ECO:0000255}. FT TRANSMEM 442 462 Helical. {ECO:0000255}. FT TOPO_DOM 463 551 Cytoplasmic. {ECO:0000255}. FT DOMAIN 19 136 Ig-like V-type. FT DOMAIN 146 229 Ig-like C2-type 1. FT DOMAIN 236 330 Ig-like C2-type 2. FT MOTIF 518 523 ITIM motif. FT MOTIF 542 547 SLAM-like motif. FT BINDING 119 119 Sialic acid. FT {ECO:0000269|PubMed:18022638}. FT BINDING 127 127 Sialic acid. FT {ECO:0000269|PubMed:18022638}. FT BINDING 129 129 Sialic acid. FT {ECO:0000269|PubMed:18022638}. FT CARBOHYD 100 100 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 210 210 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 231 231 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 253 253 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 328 328 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 375 375 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 384 384 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 393 393 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 36 170 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18022638}. FT DISULFID 41 101 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18022638}. FT DISULFID 164 213 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18022638}. FT DISULFID 269 314 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 72 72 V -> A (in dbSNP:rs1973019). FT /FTId=VAR_014249. FT VARIANT 215 215 M -> V (in dbSNP:rs1807124). FT /FTId=VAR_014250. FT VARIANT 322 322 F -> S (in dbSNP:rs2278831). FT /FTId=VAR_014251. FT VARIANT 358 358 R -> W (in dbSNP:rs8108074). FT {ECO:0000269|PubMed:9731071}. FT /FTId=VAR_049929. FT VARIANT 499 499 P -> A (in dbSNP:rs3829655). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_020087. FT CONFLICT 309 309 E -> K (in Ref. 1; AAD50978). FT {ECO:0000305}. FT CONFLICT 388 388 A -> P (in Ref. 1; AAD50978). FT {ECO:0000305}. FT CONFLICT 403 403 S -> N (in Ref. 1; AAD50978). FT {ECO:0000305}. FT STRAND 22 24 {ECO:0000244|PDB:2ZG1}. FT STRAND 27 32 {ECO:0000244|PDB:2ZG1}. FT STRAND 37 39 {ECO:0000244|PDB:2ZG1}. FT STRAND 42 44 {ECO:0000244|PDB:2ZG1}. FT STRAND 56 62 {ECO:0000244|PDB:2ZG1}. FT HELIX 67 69 {ECO:0000244|PDB:2ZG1}. FT STRAND 72 76 {ECO:0000244|PDB:2ZG1}. FT STRAND 78 80 {ECO:0000244|PDB:2ZG2}. FT TURN 84 89 {ECO:0000244|PDB:2ZG1}. FT STRAND 90 92 {ECO:0000244|PDB:2ZG1}. FT HELIX 96 98 {ECO:0000244|PDB:2ZG1}. FT STRAND 103 105 {ECO:0000244|PDB:2ZG1}. FT HELIX 110 112 {ECO:0000244|PDB:2ZG1}. FT STRAND 114 122 {ECO:0000244|PDB:2ZG1}. FT TURN 123 125 {ECO:0000244|PDB:2ZG1}. FT STRAND 126 129 {ECO:0000244|PDB:2ZG1}. FT STRAND 135 140 {ECO:0000244|PDB:2ZG1}. FT STRAND 147 149 {ECO:0000244|PDB:2ZG1}. FT STRAND 160 165 {ECO:0000244|PDB:2ZG1}. FT STRAND 171 174 {ECO:0000244|PDB:2ZG2}. FT STRAND 177 183 {ECO:0000244|PDB:2ZG1}. FT STRAND 186 188 {ECO:0000244|PDB:2ZG1}. FT TURN 190 193 {ECO:0000244|PDB:2ZG2}. FT STRAND 195 200 {ECO:0000244|PDB:2ZG1}. FT TURN 204 208 {ECO:0000244|PDB:2ZG2}. FT STRAND 210 216 {ECO:0000244|PDB:2ZG1}. FT STRAND 225 229 {ECO:0000244|PDB:2ZG1}. SQ SEQUENCE 551 AA; 60715 MW; 2FEA2B6B341EFEAF CRC64; MLPLLLLPLL WGGSLQEKPV YELQVQKSVT VQEGLCVLVP CSFSYPWRSW YSSPPLYVYW FRDGEIPYYA EVVATNNPDR RVKPETQGRF RLLGDVQKKN CSLSIGDARM EDTGSYFFRV ERGRDVKYSY QQNKLNLEVT ALIEKPDIHF LEPLESGRPT RLSCSLPGSC EAGPPLTFSW TGNALSPLDP ETTRSSELTL TPRPEDHGTN LTCQMKRQGA QVTTERTVQL NVSYAPQTIT IFRNGIALEI LQNTSYLPVL EGQALRLLCD APSNPPAHLS WFQGSPALNA TPISNTGILE LRRVRSAEEG GFTCRAQHPL GFLQIFLNLS VYSLPQLLGP SCSWEAEGLH CRCSFRARPA PSLCWRLEEK PLEGNSSQGS FKVNSSSAGP WANSSLILHG GLSSDLKVSC KAWNIYGSQS GSVLLLQGRS NLGTGVVPAA LGGAGVMALL CICLCLIFFL IVKARRKQAA GRPEKMDDED PIMGTITSGS RKKPWPDSPG DQASPPGDAP PLEEQKELHY ASLSFSEMKS REPKDQEAPS TTEYSEIKTS K //