SIG14_HUMAN
ID SIG14_HUMAN Reviewed; 396 AA.
AC Q08ET2; Q6UXG0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sialic acid-binding Ig-like lectin 14;
DE Short=Siglec-14;
DE Flags: Precursor;
GN Name=SIGLEC14; ORFNames=UNQ294/PRO333;
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 [MRNA], FUNCTION, INTERACTION WITH TYROBP, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-362.
RX PubMed=17012248; DOI=10.1096/fj.06-5800com;
RA Angata T., Hayakawa T., Yamanaka M., Varki A., Nakamura M.;
RT "Discovery of Siglec-14, a novel sialic acid receptor undergoing concerted
RT evolution with Siglec-5 in primates.";
RL FASEB J. 20:1964-1973(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-396.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
CC -!- FUNCTION: Putative adhesion molecule. Sialic acid-binding paired
CC receptor which may activate associated receptors.
CC {ECO:0000269|PubMed:17012248}.
CC -!- SUBUNIT: Interacts with TYROBP. {ECO:0000269|PubMed:17012248}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17012248};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17012248}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues including
CC bone marrow, spleen and fetal liver. Also detected in lung and testis.
CC {ECO:0000269|PubMed:17012248}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
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DR EMBL; AY854038; AAX47338.1; -; mRNA.
DR EMBL; AY358369; AAQ88735.1; -; mRNA.
DR CCDS; CCDS42604.1; -.
DR RefSeq; NP_001092082.1; NM_001098612.1.
DR AlphaFoldDB; Q08ET2; -.
DR BMRB; Q08ET2; -.
DR SMR; Q08ET2; -.
DR IntAct; Q08ET2; 1.
DR STRING; 9606.ENSP00000354090; -.
DR ChEMBL; CHEMBL4523280; -.
DR GlyConnect; 1978; 9 N-Linked glycans (5 sites).
DR GlyGen; Q08ET2; 5 sites, 9 N-linked glycans (5 sites).
DR BioMuta; SIGLEC14; -.
DR DMDM; 121940125; -.
DR MassIVE; Q08ET2; -.
DR PaxDb; Q08ET2; -.
DR PeptideAtlas; Q08ET2; -.
DR PRIDE; Q08ET2; -.
DR ProteomicsDB; 58696; -.
DR Antibodypedia; 49565; 141 antibodies from 23 providers.
DR DNASU; 100049587; -.
DR Ensembl; ENST00000360844.7; ENSP00000354090.5; ENSG00000254415.4.
DR GeneID; 100049587; -.
DR KEGG; hsa:100049587; -.
DR MANE-Select; ENST00000360844.7; ENSP00000354090.5; NM_001098612.3; NP_001092082.1.
DR UCSC; uc002pxf.5; human.
DR CTD; 100049587; -.
DR DisGeNET; 100049587; -.
DR GeneCards; SIGLEC14; -.
DR HGNC; HGNC:32926; SIGLEC14.
DR HPA; ENSG00000254415; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 618132; gene.
DR neXtProt; NX_Q08ET2; -.
DR OpenTargets; ENSG00000254415; -.
DR PharmGKB; PA162403331; -.
DR VEuPathDB; HostDB:ENSG00000254415; -.
DR eggNOG; ENOG502S41V; Eukaryota.
DR GeneTree; ENSGT01040000240469; -.
DR HOGENOM; CLU_024444_6_1_1; -.
DR InParanoid; Q08ET2; -.
DR OMA; NFLGPRT; -.
DR OrthoDB; 1049114at2759; -.
DR PhylomeDB; Q08ET2; -.
DR TreeFam; TF332441; -.
DR PathwayCommons; Q08ET2; -.
DR Reactome; R-HSA-2172127; DAP12 interactions.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q08ET2; -.
DR BioGRID-ORCS; 100049587; 119 hits in 1060 CRISPR screens.
DR ChiTaRS; SIGLEC14; human.
DR GenomeRNAi; 100049587; -.
DR Pharos; Q08ET2; Tbio.
DR PRO; PR:Q08ET2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q08ET2; protein.
DR Bgee; ENSG00000254415; Expressed in blood and 95 other tissues.
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; IBA:GO_Central.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
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 Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
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; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lectin; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..396
FT /note="Sialic acid-binding Ig-like lectin 14"
FT /id="PRO_0000309314"
FT TOPO_DOM 17..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..136
FT /note="Ig-like V-type"
FT DOMAIN 146..229
FT /note="Ig-like C2-type 1"
FT DOMAIN 236..331
FT /note="Ig-like C2-type 2"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 274..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 362
FT /note="R->A: Loss of interaction with TYROBP."
FT /evidence="ECO:0000269|PubMed:17012248"
SQ SEQUENCE 396 AA; 43970 MW; 1C2DF3C6D43C6CE0 CRC64;
MLPLLLLPLL WGGSLQEKPV YELQVQKSVT VQEGLCVLVP CSFSYPWRSW YSSPPLYVYW
FRDGEIPYYA EVVATNNPDR RVKPETQGRF RLLGDVQKKN CSLSIGDARM EDTGSYFFRV
ERGRDVKYSY QQNKLNLEVT ALIEKPDIHF LEPLESGRPT RLSCSLPGSC EAGPPLTFSW
TGNALSPLDP ETTRSSELTL TPRPEDHGTN LTCQVKRQGA QVTTERTVQL NVSYAPQNLA
ISIFFRNGTG TALRILSNGM SVPIQEGQSL FLACTVDSNP PASLSWFREG KALNPSQTSM
SGTLELPNIG AREGGEFTCR VQHPLGSQHL SFILSVQRSS SSCICVTEKQ QGSWPLVLTL
IRGALMGAGF LLTYGLTWIY YTRCGGPQQS RAERPG
