ID SIG16_HUMAN Reviewed; 481 AA. AC A6NMB1; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 3. DT 16-JAN-2019, entry version 86. DE RecName: Full=Sialic acid-binding Ig-like lectin 16; DE Short=Siglec-16; DE AltName: Full=Siglec-P16; DE Flags: Precursor; GN Name=SIGLEC16; Synonyms=SIGLECP16; 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 [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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP IDENTIFICATION. RX PubMed=11986327; DOI=10.1074/jbc.M202833200; RA Angata T., Kerr S.C., Greaves D.R., Varki N.M., Crocker P.R., RA Varki A.; RT "Cloning and characterization of human Siglec-11. A recently evolved RT signaling molecule that can interact with SHP-1 and SHP-2 and is RT expressed by tissue macrophages, including brain microglia."; RL J. Biol. Chem. 277:24466-24474(2002). RN [4] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=18629938; DOI=10.1002/eji.200738078; RA Cao H., Lakner U., de Bono B., Traherne J.A., Trowsdale J., RA Barrow A.D.; RT "SIGLEC16 encodes a DAP12-associated receptor expressed in macrophages RT that evolved from its inhibitory counterpart SIGLEC11 and has RT functional and non-functional alleles in humans."; RL Eur. J. Immunol. 38:2303-2315(2008). CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid CC dependent binding to cells. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18629938}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18629938}. CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, fetal brain, fetal CC liver, lung and salivary gland. Detected in brain, macrophage, CC cancerous esophagus and lung at protein level. CC {ECO:0000269|PubMed:18629938}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC CC (sialic acid binding Ig-like lectin) family. {ECO:0000305}. CC -!- CAUTION: According to PubMed:18629938, the SIGLECP16 sequence, CC that was initially classified as a pseudogene, has a 4 bp deletion CC when compared with the sequence shown in this entry. This deletion CC is a polymorphism with a frequency of around 50% in the UK CC population. The frameshifted allele is non-functional whereas the CC sequence displayed here seems to be functional. The functional CC allele has been named SIGLEC16 in PubMed:18629938. {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; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC039008; -; NOT_ANNOTATED_CDS; mRNA. DR UniGene; Hs.568076; -. DR UniGene; Hs.738007; -. DR ProteinModelPortal; A6NMB1; -. DR BioMuta; HGNC:24851; -. DR EPD; A6NMB1; -. DR jPOST; A6NMB1; -. DR MaxQB; A6NMB1; -. DR PRIDE; A6NMB1; -. DR ProteomicsDB; 1527; -. DR GeneCards; SIGLEC16; -. DR H-InvDB; HIX0040097; -. DR HGNC; HGNC:24851; SIGLEC16. DR neXtProt; NX_A6NMB1; -. DR HOGENOM; HOG000236324; -. DR HOVERGEN; HBG036161; -. DR InParanoid; A6NMB1; -. DR PhylomeDB; A6NMB1; -. DR TreeFam; TF332441; -. DR Reactome; R-HSA-2172127; DAP12 interactions. DR PRO; PR:A6NMB1; -. DR Proteomes; UP000005640; Unplaced. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0089717; C:spanning component of membrane; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0098740; P:multi organism cell adhesion; IDA:UniProtKB. DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:UniProtKB. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB. 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; IPR003006; Ig/MHC_CS. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF07679; I-set; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 4. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF48726; SSF48726; 4. DR PROSITE; PS50835; IG_LIKE; 3. PE 2: Evidence at transcript level; KW Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Lectin; Membrane; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 16 {ECO:0000255}. FT CHAIN 17 481 Sialic acid-binding Ig-like lectin 16. FT /FTId=PRO_0000332258. FT TOPO_DOM 17 434 Extracellular. {ECO:0000255}. FT TRANSMEM 435 455 Helical. {ECO:0000255}. FT TOPO_DOM 456 481 Cytoplasmic. {ECO:0000255}. FT DOMAIN 19 122 Ig-like V-type. FT DOMAIN 147 232 Ig-like C2-type 1. FT DOMAIN 238 322 Ig-like C2-type 2. FT DOMAIN 327 424 Ig-like C2-type 3. FT BINDING 120 120 Sialic acid. {ECO:0000250}. FT CARBOHYD 43 43 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 78 78 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 338 338 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 347 347 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 37 174 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 42 102 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 165 216 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 259 306 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 363 408 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 481 AA; 52992 MW; 72C6D2D759F94BBC CRC64; MLLLPLLLPV LGAGSLNKDP SYSLQVQRQV PVPEGLCVIV SCNLSYPRDG WDESTAAYGY WFKGRTSPKT GAPVATNNQS REVAMSTRDR FQLTGDPGKG SCSLVIRDAQ REDEAWYFFR VERGSRVRHS FLSNAFFLKV TALTQKPDVY IPETLEPGQP VTVICVFNWA FKKCPAPSFS WTGAALSPRR TRPSTSHFSV LSFTPSPQDH DTDLTCHVDF SRKGVSAQRT VRLRVASLEL QGNVIYLEVQ KGQFLRLLCA ADSQPPATLS WVLQDRVLSS SHPWGPRTLG LELPGVKAGD SGRYTCRAEN RLGSQQRALD LSVQYPPENL RVMVSQANRT VLENLRNGTS LRVLEGQSLR LVCVTHSSPP ARLSWTWGEQ TVGPSQPSDP GVLQLPRVQM EHEGEFTCHA RHPLGSQRVS LSFSVHCKSG PMTGVVLVAV GEVAMKILLL CLCLILLRVR SCRRKAARAA LGMEAADAVT D //