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Database: UniProt
Entry: W5N581_LEPOC
LinkDB: W5N581_LEPOC
Original site: W5N581_LEPOC 
ID   W5N581_LEPOC            Unreviewed;      1995 AA.
AC   W5N581;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Sidekick cell adhesion molecule 2 {ECO:0000313|Ensembl:ENSLOCP00000015790.1};
GN   Name=SDK2 {ECO:0000313|Ensembl:ENSLOCP00000015790.1};
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:ENSLOCP00000015790.1, 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:ENSLOCP00000015790.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01000375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000015790; -.
DR   Ensembl; ENSLOCT00000015820.1; ENSLOCP00000015790.1; ENSLOCG00000012818.1.
DR   eggNOG; KOG3510; Eukaryota.
DR   eggNOG; KOG4221; Eukaryota.
DR   GeneTree; ENSGT00940000155761; -.
DR   InParanoid; W5N581; -.
DR   OMA; WFMVTLA; -.
DR   Proteomes; UP000018468; Linkage group LG10.
DR   Bgee; ENSLOCG00000012818; Expressed in camera-type eye and 7 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 13.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 17.
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; PROTEIN SIDEKICK; 1.
DR   PANTHER; PTHR44170:SF46; PROTEIN SIDEKICK-1 ISOFORM X1; 1.
DR   Pfam; PF00041; fn3; 13.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 13.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 7.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50853; FN3; 13.
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        1732..1755
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..99
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          110..200
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          204..293
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          298..389
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          394..490
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          495..591
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          596..695
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          699..793
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          797..896
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          901..999
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1004..1101
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1105..1199
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1204..1301
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1306..1423
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1428..1524
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1528..1623
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1626..1724
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          480..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1811..1830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1842..1870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1898..1995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1842..1862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1914..1931
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1932..1978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1995 AA;  219852 MW;  4B05A125AB3ACD57 CRC64;
     PVTLTENVGG PADPIAPTII IPPRNTSVIS GTSEVTMECV ANARPLIKLS ISWRKDGVLV
     TSGLSDFNRQ LTILSPAVSD AGFYECEAIL RSSSVPSVSA GAYLHVLEPP QFVKEPDRHI
     TAEMEKVVDI PCQARGVPQP EIVWYKDAVP VSHVKTLRYR VLSGGSLQVN GLLPDDTGMF
     QCFARNPAGE VQTNTYLAVT SIAPNITAGP SDSTVIDGMS VILHCETSGA PRPAITWQKG
     ERILASGSVQ LPRFTLLESG SLLISPSHIS DAGTYTCMAS NSRGIDEASA ELVVWARTRI
     TSPPQDQSVI KGTKAILTCG VTHDPSVTVR YTWEKGSSVI NPDSVPRIRM DPDGTLHISQ
     TWSGDIGTYT CHVTSVGGND SRSAHLRVRQ LPHAPENPVA TLSLIEKRAI NLTWAKPFDG
     NSPLIRYILE VSENNAPWTV LLANIEPESN MVTVGGLIPA RSYQFRICAV NDVGKGQFSK
     ETDRLSLPEE PPSAPPQNVI ASGRTNQSIM IQWQPPPETH QNGILRGYII RYCLAGLPVE
     YQFKNITNPD VTNLLLEDLI IWTNYEIEVA AYNGAGLGVY SHTVTEWTLQ GVPTVPPGNV
     QAEAVNSTTV RFTWTPPSPQ FINGINQGYK LLAWEPGKEE EVTVVTVRPN FQDNVHVGYI
     TGLKKFTEYF SSVLCFTTPG DGPRSASHAL RTHEDIPGAV GHLSFTEILD TSLKVSWREP
     NEKNGILTGY RISWEEYNRT NTRVTHYLPN VTLEYRVTGL TALTTYTIEV AAMTSKGQGQ
     LSSSTISSGV PPELPGPPTN MAISNIGPRS VTLQFKPGYD GKTSISRWQV EAQITVIGEN
     EEWVLVHQVP NEPDARSLEV PNLNPYTFYR FRMRQVNIVG TSPPSQPSRK IQTLQAPPDI
     APANVTLRTA SETSLWLRWV PLPEWEYNGN PEFVGYRVQY SRTGAQGRAL THVIQDRLER
     EFTIEDLEEW TEYEVRVQAL NGIGAGPWSQ PVRGRTRESV PSCGPTNITA FATTSSSILI
     RWHEVPEPDR NGLILGYKVV YKEKDSDSPL RFWTVEGNAT QSVQLTGLGK YVLYQIQVLA
     FTRIGDGVPS KPPILERTLD DVPGPPVGIL FPEVRTNSVR LIWQSPAQPN GIILAYQITY
     RLNSTSSNTA TVEVLNPSTR QFTVTGLKPE SVYVFRITAQ TRKGWGEVAE ALVVTTEKRA
     RPQPTSRPTV QQENVQARSV LLSWEPGSDG LSPVRYYTVQ LRELPNKNWT VHSASVSHEA
     TSYIVNRLKP FTSYQFRVKA TNDIGDSEYS EESEAITTLQ DAPDAAPVIL SVTPHTTTSV
     LIRWQPPSEE HINGILLGFR IHYRELLYER LRSFTVRTFN GPTATWAELT SPYSVRNLTE
     SSLTQYELDN LSKHKRYEIR LSVYNAVGEG PTSAPQEVFV GEAVPTAPPQ NVAIQSATAT
     QLDVTWDPPP LEAQNGDIQG YKIYFWEFQR QNQTERLRTL FLPEGGVKLK NLTGYTTYMI
     SVAAFNAAGD GPRSPATRGR TQQAAPSAPS FIHFSELTTT SVNVSWGEPV HPNGIIEGYR
     LIYEPCTPVD GVSKIVTVDV KGSAPLWMKI KDLADGVTYN FRIRAKTFAY GPEVEANITT
     GPGEGAPGPP GEPFISRYGS ALTLHWANGD PGRAPITRYV IEARPSDEGL WDILIKDIPK
     EVTSYTFNMD ILKQGVSYDF RVIGVNDYGY GSPSAPSPSI SAQKVAPFYE EWWFLVVVAL
     VGLIFILLLV FILIIRGQSK KYAKKSDSGN NSNCNALSHG EMVSLDEGRF PALELNNRRL
     SVKNSFCRKN GVYTRSPPRP SPGSLHYSDE DVSTKYNDLI PAESSSLTEK PSEISDSQGS
     DSEYEVDQNR QKTHSFVNHY ISDPTYYNSW RRQQKGISRA QAYSYTESDS GEPEHCAPPP
     PLPPLPPLPP QLNNTAQAQA QAQAQGSLFR PKGSRTPTPQ QQPSNPPSQH STLYRPPSSL
     APGSRAPIAG FSSFV
//
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