ID A0A1S3G318_DIPOR Unreviewed; 608 AA.
AC A0A1S3G318;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Sialic acid-binding Ig-like lectin 10 {ECO:0000313|RefSeq:XP_012883060.1};
GN Name=LOC105994177 {ECO:0000313|RefSeq:XP_012883060.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883060.1};
RN [1] {ECO:0000313|RefSeq:XP_012883060.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883060.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_012883060.1; XM_013027606.1.
DR AlphaFoldDB; A0A1S3G318; -.
DR GeneID; 105994177; -.
DR KEGG; dord:105994177; -.
DR InParanoid; A0A1S3G318; -.
DR OrthoDB; 2963061at2759; -.
DR Proteomes; UP000081671; 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 CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR PANTHER; PTHR12035:SF115; SIALIC ACID-BINDING IG-LIKE LECTIN 10; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
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:UP000081671};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010359974"
FT TRANSMEM 489..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 152..238
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 266..358
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 377..474
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 519..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 65936 MW; 1090617D7E332C9F CRC64;
MQRLNTQLCL SLLLLSLGGS QAQKPGYKVQ VQSLVKVQEG LWVLVPCSFS YPSQEAGLDS
SQAHGYWFTE GTNTDTGEPV ASTNPARPTQ GWTQGRFQLL GDPHRNDCTL FIRDAQKEDK
KNYFFRVEKG EKLKYNFLVD MFRLEVTALT QPHIFIPETL EPGRAVTIIC MVPCISQQCV
APSISWSGPA LSSTESRPQT SFLSAISLTP RLRDHGTQLT CRADFRAGNT VENTVRLSVA
CAPRDLVITI LHDNAQGGRS SGRAGPTLEK WKAQESKGNM TCVDVRKGQF LRLLCTAAGW
PPPTMTWVLG NQVLLRSNAT HPGNLGLDLP RVKVRDAGRY TCHAENRLGS QRHSLNVCVQ
CAGRGSPGHC VSIADSPEAL TVTASQGNST ELEIHRNGSS LHVLQGQSLR LVCVTHSHPT
ATLTWTQGSK MLSPPWPAEP GVLELPMVQA EHEGEFTCRA QNPLGDLHIS LSLSVHYEGS
ISAAFSKGAG LGIGATSLLF LCLIVLIVKM LRKSQPHTET CRTHVSPHST VLDNSIVNPK
ARVPKKKAKP SSPPRTASPG AGSPEPRKKE KAALSCPEPA SPTQDPDSET ARKKSIMLLS
TSPGLLRS
//
