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Database: UniProt
Entry: U6D2W0_NEOVI
LinkDB: U6D2W0_NEOVI
Original site: U6D2W0_NEOVI 
ID   U6D2W0_NEOVI            Unreviewed;       383 AA.
AC   U6D2W0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sialic acid-binding Ig-like lectin 5 {ECO:0000313|EMBL:CCP76417.1};
DE   Flags: Fragment;
GN   Name=SIGL5 {ECO:0000313|EMBL:CCP76417.1};
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP76417.1};
RN   [1] {ECO:0000313|EMBL:CCP76417.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pool of brain {ECO:0000313|EMBL:CCP76417.1};
RA   Anistoroaei R., Christensen K.;
RT   "An American mink transcriptome.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; HAAF01004592; CCP76417.1; -; mRNA.
DR   AlphaFoldDB; U6D2W0; -.
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; 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:SF103; SIALIC ACID-BINDING IG-LIKE LECTIN 5; 1.
DR   Pfam; PF07679; I-set; 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.
PE   2: Evidence at transcript level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000313|EMBL:CCP76417.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..383
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004669254"
FT   DOMAIN          145..228
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          263..328
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   NON_TER         383
FT                   /evidence="ECO:0000313|EMBL:CCP76417.1"
SQ   SEQUENCE   383 AA;  42941 MW;  4A0F5E801D2A4E19 CRC64;
     MVSLLLLPLL WGGSLQEDWG YELQVQDTVT VQEGLCVYVP CSFSYPWSSW PTHERPYMYW
     FRSGDSFHNS QPVATNDPTK LVKTEFWGRF NLIRKPREND CSLRIREARR SDQGLYKFHI
     AKDYGRYTYK DKQLNLQVAA LTQEPDIHFP EPMKSGYATN LTCSLQGSCE EGRPLSFFWV
     GGALDSLDRQ TLRSSVLTLT PRVQDHGSNL TCQVHLPEGQ GTVKRTIRLN VSYAPQNLTI
     SLLSSDVTAL KILEKGLIIL PQEGQTPQLL CVAEGNPPAQ LSWVLGGQTL SPSQPTDPGI
     LELPQIQLEH EGDLTCQAQN LLGSRQVSLH LSVVYPPQLL SLSCSWEGEG LHCNCSSRAQ
     PAPTLHWRLG EELLEGNHSN ASW
//
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