ID W5LY09_LEPOC Unreviewed; 1122 AA.
AC W5LY09;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Cell adhesion associated, oncogene regulated {ECO:0000313|Ensembl:ENSLOCP00000001016.1};
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:ENSLOCP00000001016.1, 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:ENSLOCP00000001016.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01023945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015193014.1; XM_015337528.1.
DR AlphaFoldDB; W5LY09; -.
DR Ensembl; ENSLOCT00000001020.1; ENSLOCP00000001016.1; ENSLOCG00000000869.1.
DR GeneID; 102696609; -.
DR KEGG; loc:102696609; -.
DR CTD; 50937; -.
DR GeneTree; ENSGT00940000157114; -.
DR HOGENOM; CLU_008503_0_0_1; -.
DR OrthoDB; 3138076at2759; -.
DR Proteomes; UP000018468; Linkage group LG26.
DR Bgee; ENSLOCG00000000869; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
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:SF1; CELL ADHESION MOLECULE-RELATED_DOWN-REGULATED BY ONCOGENES; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 3.
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 861..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..133
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 135..223
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 242..324
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 334..419
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 474..575
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 619..715
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 723..823
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 428..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 120192 MW; F2AC50AE3E7014BE CRC64;
MRCLLGSRDR PVERACAMDS SLGALPRLVC LSLSLASILG CSCARLSFRE EPVSATQRPG
GPVLLRCSAQ PEEARVSWLW EGRPLDPAAL PPELELRPGA LAIRALHPPH TGRYFCVAQL
GSRAIASRNA HITIAEISAF RDLPRRLVKA EEGGTALIRC QLPPSTPPAV PRFRVRGQWL
EQSTGDFFIF PSGSLQIRAV SPQHQGTYRC GAHNPVTQET RLEPHGQRLA VTRPADPAAP
APLRIVYPTS PQTVSVVKAQ PLVLECIVAG RPAPAVRWTR EGRQVALGPG RRLQHHSLVL
DSAARSDGGA YRCSARDQTG RVVSADYTVE VLEPASVSQG LSDRSVSVGS SVNFTCASRG
NPAPNVTWLL DSAPLAPSPR LQLSGSSLRI ASAGPQDQGV YQCLVDNGIG SAQSSGMLTV
QSAPLETSTV GVAPEAPPSA HPVQSDEGEE PPAQEEGLGG SLAPPTERTS DTPTPEAPII
TSPPQTHKPD VYDLEWRAGR DWGSPIIAYF VKYRKLDEMG TVLGGWHTVR VPGSEKALRL
SELEPSSLYE VLMVARSAGG DGQPAMLTFR TGKERSGPSS RSPHPQGPSP PAGRPEKLPA
SEALNTHFGV VVHDRVPEAP DRPTISMATE SSVYVTWIPR ANGGSPITAF RVEYRKQGRS
ADWVPAADNI SPLKLSVEVR SLEPGATYRF RVIAINTYGE SPHSAPSRPY HVPAVSTHFT
TRPVAGPHIS STDAVSDTQI ILRWTYTPSS NNNTPIQGFY IYYRPTDSDN DSDYKRDVVE
GNKQWHLIGQ LQPETSYDIK MQCFNDGGES EYSNVMICET KARQAPGVSP GGGAGAVTPP
GPPERGGGGA GGVQSQRGGD MLYLIVGSVL GVMVLILLAF IAMCLWRSRQ QSSLHKYDPP
GYLYQPAEMS SHVLEYAALP GTSHANGGLR PLPGGCPHLH HKLPGGPPLL AGAHRPHNGG
GVYTALPQSD PSDCMSCQNF CNNNRCYTKT NGTFSNGTLP MMHHMSPCQQ DGLEMMPLAH
VTPGCDTPTV PQCPGELGEE GEKGSMTLPP SQHSCCQAGE YCQLGGRGEE LHCREAEGPV
LVCWETRGPP VLDCPETAGW ISTGTAMDRA LGDFSQPELL ET
//
