ID L5LMR4_MYODS Unreviewed; 633 AA.
AC L5LMR4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Sialic acid-binding Ig-like lectin 5 {ECO:0000313|EMBL:ELK26783.1};
GN ORFNames=MDA_GLEAN10000678 {ECO:0000313|EMBL:ELK26783.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26783.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB110811; ELK26783.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LMR4; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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; 5.
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 PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR PANTHER; PTHR12035:SF103; SIALIC ACID-BINDING IG-LIKE LECTIN 5; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
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, ECO:0000313|EMBL:ELK26783.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..633
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003970438"
FT TRANSMEM 609..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..353
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 418..503
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 633 AA; 69938 MW; 536C15BC921A2FEB CRC64;
MVTLLLLLLL SGESLEEHPG FELQVQESVT VQEGLCVHVP CSFSYPWNSR SSSSELYTYW
YWKEDSIWYS PPVASNDPNK PAKGENQGRF LLPDARNNNC SLHIRDARRS DTGIYIFRME
RGSVKYNYQD KMLNLQVTGS LQQQSGFELQ VQESMTVQEG LCVHVPCSFS YPWSSWSSSS
KFYTYWYWKE DNMQYSKPVA SNNPNKPAKE ETKSRFLLPD TRSNNCSLHI RDARRSDAKI
YVFRMERESM KYTYKEKMLN LQVTALREKP HIRVREPLES GHPTQLACSL SGACKGGRPL
TFSWAGAAVD SLDPQNLSSS VLTFTPRPGD HGTNLTCQVK REGSQWTTQR TIQLDVSYAP
QNLIIGVSFR KDTGRKEPLL SGLGPAPGPW WGRGGSRRLN GMRHGKGRDE SHHPSPAPLV
AYKNLQTTSL SILEGEALRL LCEADSNPPA ELSWFRGSPG LNATPLSSTA ILELPRVGPA
QEGEFTCQAR HRLGSHRVSL SLSVVYPPQL LGPSCSWEDQ GLHCSCSSRA QPAPSLHWRL
GAGLLEGNHG NASHVVSSSS EGPWTNSSLS IKEGLSPDLR LSCEAWNVQG AQSASVLLLP
GKAVPQTGVV PVALGGAGAL ALLSLCLCLI FCM
//