ID A0A3Q7SZU8_VULVU Unreviewed; 550 AA.
AC A0A3Q7SZU8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=LOW QUALITY PROTEIN: sialic acid-binding Ig-like lectin 5 {ECO:0000313|RefSeq:XP_025869999.1};
GN Name=LOC112931493 {ECO:0000313|RefSeq:XP_025869999.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025869999.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025869999.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025869999.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025869999.1};
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_025869999.1; XM_026014214.1.
DR STRING; 9627.ENSVVUP00000015281; -.
DR KEGG; vvp:112931493; -.
DR OrthoDB; 5350608at2759; -.
DR Proteomes; UP000286640; 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; 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:SF99; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 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:UP000286640};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..550
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018704156"
FT TRANSMEM 442..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 229..326
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 475..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 60064 MW; 76E5AA9EC6193198 CRC64;
MMILRLXLSW GLARASGSSS ELQLELQESV TVQEGLCVHV PCKFSYPWLA FIGSHMFWFQ
KGADVDHDPP VATNIPSQKL HERTQGRFFL RGNPQAQDCS LDIIEVNMGD SGTYFFQIGK
YSYLDNMLSL NVTALTHTPD ILIPRTLESS HPRNLTCSVP WACEQGMAPI FSWTSAALTS
PGPRTHLSSV LILSPRPQDH GTNLTCQVYF PAADVMVGRT IQLNVTYAPQ NTAIRIFQGN
RTVLETLQNT SSILILEGQA LQLLCAADSN PPAELSWFRG SPALNATPIY RSPILDLPQV
GTAEEGDFTC RAQNSLGSQH VSLHLSVVYP PRPLSPSCSW EGEALQCTCS SHALPAPTLR
WRLGEGLLER NHSNASLTVT SSAEGPWANS SLSLRGPLGS GLRLSCEAWN AHGKQSAAVL
LLPVKKFLNS NSVGKSEPRT SGVLGAVGGA GSMALLSLCL CLIFRVKTRR KKAAQPVQSM
DMSPDDSSDS GAHQDQSWMD IPEDHPAPAG ASPTSREEQE LHYAFLQFPK LKLREQESIN
TEYSEIKTHK
//