SIG12_PANTR
ID SIG12_PANTR Reviewed; 597 AA.
AC Q95LH0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Sialic acid-binding Ig-like lectin 12;
DE Short=Siglec-12;
DE AltName: Full=Sialic acid-binding Ig-like lectin-like 1;
DE Short=Siglec-L1;
DE Flags: Precursor;
GN Name=SIGLEC12; Synonyms=SIGLECL1;
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=11546777; DOI=10.1074/jbc.m105926200;
RA Angata T., Varki N.M., Varki A.;
RT "A second uniquely human mutation affecting sialic acid biology.";
RL J. Biol. Chem. 276:40282-40287(2001).
CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC dependent binding to cells. The sialic acid recognition site may be
CC masked by cis interactions with sialic acids on the same cell surface.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
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DR EMBL; AF293372; AAL09302.1; -; mRNA.
DR RefSeq; NP_001009040.1; NM_001009040.1.
DR AlphaFoldDB; Q95LH0; -.
DR STRING; 9598.ENSPTRP00000054309; -.
DR GeneID; 450120; -.
DR KEGG; ptr:450120; -.
DR CTD; 27181; -.
DR InParanoid; Q95LH0; -.
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; -; 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; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 1.
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; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..597
FT /note="Sialic acid-binding Ig-like lectin 12"
FT /id="PRO_0000014955"
FT TOPO_DOM 21..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..144
FT /note="Ig-like V-type 1"
FT DOMAIN 145..271
FT /note="Ig-like V-type 2"
FT DOMAIN 277..360
FT /note="Ig-like C2-type 1"
FT DOMAIN 367..464
FT /note="Ig-like C2-type 2"
FT REGION 514..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 565..570
FT /note="ITIM motif"
FT MOTIF 588..593
FT /note="SLAM-like motif"
FT MOD_RES 567
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y57"
FT MOD_RES 590
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y57"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 168..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 173..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 295..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 403..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 597 AA; 65076 MW; 74C13CFA9CDB5BA5 CRC64;
MLLLLLLLLL PPLLCGRVGA KEQKDYLLTM QKSVTVQEGL CVSVLCSFSY PQNGWTDSDP
VHGYWFRAGD HVSRNVPVAT NNPARAVQEE TRDRFHLLGD PQNKDCTLSI RDTRESDAGT
YVFRVERGNM KWNYKYDQLS VNVTASQDLL SRYRLEVPES VTVQEGLCVS VPCSVLYPHC
NWTASSPVYG SWFKEGADIP CDIPVATNTP SGKVQEDTQG RFLLLGDPQT NNCSLSIRDA
RKGDSGKYYF QVERGSRKWN YIYDKLSVHV TALTHLPTFS IPGTLESGHP RNLTCSVPWA
CEQGTPPTIT WMGASVSSLE PTISRSSMLS LIPKPQDHGT SLTCQVTLPG AGVTTTRAVR
LNISYPPQNL TMTVFQGDGT ASTTLRNGSA LSVLEGQSLH LVCAVDSNPP ARLSWTWGSL
TLSPSQSSNL GVLELPRVHV KDEGEFTCRA QNPLGSQHIS LSLSLQNEYT GKMRPISGVT
LGAVGGAGAT ALVFLSFCII FVVVRSCRKK SARPAVGVGD TGMEDTNAVR GSASQGPLIE
SPADDSPPHH APPALATPFP EEGEIQYASL SFHKARPQYP QEQEAIGYEY SEINILK
