ID   SIG13_PANTR             Reviewed;         387 AA.
AC   Q64JA4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Sialic acid-binding Ig-like lectin 13;
DE            Short=Siglec-13;
DE   Flags: Precursor;
GN   Name=SIGLEC13;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15331780; DOI=10.1073/pnas.0404833101;
RA   Angata T., Margulies E.H., Green E.D., Varki A.;
RT   "Large-scale sequencing of the CD33-related Siglec gene cluster in five
RT   mammalian species reveals rapid evolution by multiple mechanisms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13251-13256(2004).
CC   -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC       dependent binding to cells. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC       acid binding Ig-like lectin) family. {ECO:0000305}.
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DR   EMBL; AY485345; AAS55863.1; -; mRNA.
DR   RefSeq; NP_001036087.1; NM_001042622.1.
DR   AlphaFoldDB; Q64JA4; -.
DR   SMR; Q64JA4; -.
DR   STRING; 9598.ENSPTRP00000054310; -.
DR   PaxDb; Q64JA4; -.
DR   PRIDE; Q64JA4; -.
DR   GeneID; 732483; -.
DR   KEGG; ptr:732483; -.
DR   CTD; 732483; -.
DR   eggNOG; ENOG502SKMX; Eukaryota.
DR   InParanoid; Q64JA4; -.
DR   OrthoDB; 324083at2759; -.
DR   Proteomes; UP000002277; Unplaced.
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   Gene3D; 2.60.40.10; -; 3.
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; 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; 2.
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..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..387
FT                   /note="Sialic acid-binding Ig-like lectin 13"
FT                   /id="PRO_0000014952"
FT   TOPO_DOM        16..341
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          16..138
FT                   /note="Ig-like V-type"
FT   DOMAIN          144..227
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          234..326
FT                   /note="Ig-like C2-type 2"
FT   BINDING         118
FT                   /ligand="N-acetylneuraminate"
FT                   /ligand_id="ChEBI:CHEBI:35418"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        40..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        162..211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        270..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   387 AA;  42525 MW;  436E01C0F7E5E980 CRC64;
     MLPLLLPLLW AGALALEGIF QLEVPESVTV QEGLCVFVPC TFFYPRHTFI KISLACGYWF
     REGDNPLRDA PVATNDPARQ VREETRGRFR LLGNPREKNC SLSIRDARRR DSGSYFFRVE
     EAMMKYNYKD PPLSVHVTAL THRPDILIPG ALKSGRPRNL VCSVPWACEQ GTPPIFSWIG
     TSVSPLSPTT ALSSVVTLIP QPQDHGSRLT CQVTLPGAGV TTTRTVRLNV SYPPQNLTLT
     VFQGDGTAST TLRNESSLQV LEGQSLRLVC AVDSNPPARL SWAQDNLILS PSQPNPGMLE
     LPQMHLRNEG EFTCQARNPL GSQQVSLRLF VQRKSGPMAE VVLVAIGEAA VKILLLFLCL
     IILRVKSHRR KAAKAATGVE AAKVVKG