ID W5N8Q7_LEPOC Unreviewed; 1250 AA.
AC W5N8Q7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Immunoglobulin superfamily DCC subclass member 4 {ECO:0000313|Ensembl:ENSLOCP00000017016.1};
GN Name=IGDCC4 {ECO:0000313|Ensembl:ENSLOCP00000017016.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017016.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017016.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01024845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N8Q7; -.
DR Ensembl; ENSLOCT00000017046.1; ENSLOCP00000017016.1; ENSLOCG00000013791.1.
DR GeneTree; ENSGT00940000159637; -.
DR HOGENOM; CLU_006906_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000013791; Expressed in camera-type eye and 10 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 5.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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 PANTHER; PTHR44170:SF39; FI24025P1; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 944..966
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..126
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 129..221
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 233..319
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 324..409
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 419..513
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 515..612
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 621..729
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 742..835
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 840..935
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 970..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 136175 MW; 094E84BC66A540B3 CRC64;
LIVTQLLFPC ELTLKHCAHE VADKSHSVEL SCSAGPVQVV LEPTHSLVLD CNLAAVDQPV
NVSWGRDGVP VVDSEGLRVL PNGSLAILPA LQEGRAQERS LEGGYTCVSA NAFGALSSRT
VLVQLSGLSR FLQHPEPQLV PVGGAVRFEC HVDGLPPPLI TWEKDQGPLP SHPSSLSPHR
FISLPNGVLQ VVGVQEEDAG VYRCVATNSA RKRYSQDATL TIVPGRMLQE NKEVVIVAPP
RNTTVVVGKM TVMECMAQAH PTPYVSWIRQ DGKPVATDVV VLSTNLMIAD TQPHHAGVYV
CRANKPKTRE FVTAAAELRV LAPPTIFQTP ETVSLSRGNT ARFVCNSSGE PPPTLRWLKN
GEPIQSNGRV KTQSPGILLI NQIGLDDAGY YQCIAENSLG TACATAKLSV IVREGLPSAP
HIVSAQPTSS STMLLSWERP EHNNDQIIGF SVHYQKAVGS DNMEYQFAVN NDTTDFHVKD
LQPNTAYTFY VVAYSPMGAS RTSTSVTVHT LEDVPSASPQ LSLLSTSPTD IRVMWQPLSV
ELSRGSVTQY RIDYCALEEA DQVYSLEVAG NETQVTLHGL HPNKLYRVRI AAGTRAGFGA
PSEWTLHRTP ERYNHTMVLF APTELKVRAK MDSLHVTWQP PANHAQITGY KLYYQEVELE
DPANEENPES ARGGGLEGTT IRLRKKAKHY DITGLAPDQL YEVRVRAFNK HTDGYAAVWK
GRTERAPVTV GEPALRSLPP LPPTGIQATA NSSTSIWLRW EKPRFSTVRI INYTVRCSPS
GVKNASLVSY YTSNAQEILV GTLKPFMRYE LAVQSHAQGV DGPFSKVVEE STLPDRPSTP
PAELQVRPLN PHAVFVRWRP PLEPNGIIVE YNILYSENSS QPDNLWSSLS REGNTFSTEV
EGLQSATRYF FKMGAKTVVG AGPFSSVKDV HTLPETGLLD IHSVTGIIVG VCLGLLCILL
CMCVSFRSSK GRDTPGGLDS RGSSALSSQY RKGRSAPVAV PDCHELETLM SPRPEDTTLP
LTEATEVTEE QSLMGSRPAE ESLNLSLEPK SAWNGSVSRN WTNNITSYRD TITEGSPVLG
NGSMGMMTDN GVGKHHKLLY TMASNQVEAE VIVHSELSEP EGEWGDESEG SCHLSHSDGT
PPATEQLPRA PAAAEPDSQD SQEPTPKVLT NHNDRWERGK LEPSQGNGLT NGFHSPENHV
PAENRDSLQP SSRRFTPGKG LLLHPQEAPS QHAASGLINS TSTAHSYLHP
//