SIG16_HUMAN
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 03-AUG-2022, entry version 100.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 project:
RT 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., 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 expressed
RT 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., Barrow A.D.;
RT "SIGLEC16 encodes a DAP12-associated receptor expressed in macrophages that
RT evolved from its inhibitory counterpart SIGLEC11 and has functional and
RT 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}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:18629938}.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, fetal brain, fetal liver,
CC lung and salivary gland. Detected in brain, macrophage, cancerous
CC esophagus and lung at protein level. {ECO:0000269|PubMed:18629938}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:18629938, the SIGLECP16 sequence, that was
CC initially classified as a pseudogene, has a 4 bp deletion when compared
CC with the sequence shown in this entry. This deletion is a polymorphism
CC with a frequency of around 50% in the UK population. The frameshifted
CC allele is non-functional whereas the sequence displayed here seems to
CC be functional. The functional allele has been named SIGLEC16 in
CC PubMed:18629938. {ECO:0000305}.
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DR EMBL; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039008; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; A6NMB1; -.
DR SMR; A6NMB1; -.
DR IntAct; A6NMB1; 1.
DR GlyGen; A6NMB1; 4 sites.
DR BioMuta; HGNC:24851; -.
DR jPOST; A6NMB1; -.
DR MassIVE; A6NMB1; -.
DR MaxQB; A6NMB1; -.
DR PeptideAtlas; A6NMB1; -.
DR PRIDE; A6NMB1; -.
DR ProteomicsDB; 1527; -.
DR GeneCards; SIGLEC16; -.
DR HGNC; HGNC:24851; SIGLEC16.
DR neXtProt; NX_A6NMB1; -.
DR InParanoid; A6NMB1; -.
DR PhylomeDB; A6NMB1; -.
DR TreeFam; TF332441; -.
DR PathwayCommons; A6NMB1; -.
DR Reactome; R-HSA-2172127; DAP12 interactions.
DR ChiTaRS; SIGLEC16; human.
DR Pharos; A6NMB1; Tdark.
DR PRO; PR:A6NMB1; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NMB1; protein.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
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; Disulfide bond; Glycoprotein; Immunoglobulin domain; Lectin;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..481
FT /note="Sialic acid-binding Ig-like lectin 16"
FT /id="PRO_0000332258"
FT TOPO_DOM 17..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..122
FT /note="Ig-like V-type"
FT DOMAIN 147..232
FT /note="Ig-like C2-type 1"
FT DOMAIN 238..322
FT /note="Ig-like C2-type 2"
FT DOMAIN 327..424
FT /note="Ig-like C2-type 3"
FT BINDING 120
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 42..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 363..408
FT /evidence="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
