ID A0A2K5XY19_MANLE Unreviewed; 391 AA.
AC A0A2K5XY19;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Sialic acid binding Ig like lectin 6 {ECO:0000313|Ensembl:ENSMLEP00000008204.1};
GN Name=SIGLEC6 {ECO:0000313|Ensembl:ENSMLEP00000008204.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000008204.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000008204.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000256|ARBA:ARBA00038361}.
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DR AlphaFoldDB; A0A2K5XY19; -.
DR Ensembl; ENSMLET00000031583.1; ENSMLEP00000008204.1; ENSMLEG00000028212.1.
DR GeneTree; ENSGT01080000257333; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
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 InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR PANTHER; PTHR12035:SF129; SIALIC ACID-BINDING IG-LIKE LECTIN 6; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..391
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014348745"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..233
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 251..346
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 391 AA; 42841 MW; 1C5C85C964337DA0 CRC64;
TQGAQEAASE MLPLLLLLLW AGALAWEQRF RLEGPELLTV QEGLCVLLPC RLPPIYSLRY
IYYGYWFLEG ADVPVATNDP HEEVQEETRG RFHLLWDLSS KNCSLRIRDA RRRDTAVYFF
QLKQKWPNFG YTSYVSSKLS VCVLALTHRP SISIPGTLES GCSRTLNCSV PWACEQGTPP
IFSWMSAAPT SLGPRTTQSS VLTITPRPQD HSTNLTCQVT FPGVGVTMER TIQLNVSWML
RLPPLSTPDA PQKVTVSIFQ GNSTALKILQ NTSSLPVLEG QALRLLCDAD GNPPAHLSWF
RGFPALNATL ISNTGVLELS QVGSAEEGGF TCRAQHPLGS LQISLSLFVQ WKPEGGVSGV
LGAVWGAGTT ALVFLCVGFI FRVISTSSRE A
//
