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Database: UniProt
Entry: A0A1L8G2U4_XENLA
LinkDB: A0A1L8G2U4_XENLA
Original site: A0A1L8G2U4_XENLA 
ID   A0A1L8G2U4_XENLA        Unreviewed;      1736 AA.
AC   A0A1L8G2U4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-JUN-2019, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OCT78150.1};
GN   ORFNames=XELAEV_18029258mg {ECO:0000313|EMBL:OCT78150.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:OCT78150.1, ECO:0000313|Proteomes:UP000186698};
RN   [1] {ECO:0000313|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000313|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J.,
RA   Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
RA   Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
RA   Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
RA   van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
RA   Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
RA   Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
RA   Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
RA   Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
RA   Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
RA   DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Veenstra G.J., Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   EMBL; CM004475; OCT78150.1; -; Genomic_DNA.
DR   Proteomes; UP000186698; Chromosome 5s.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   Pfam; PF00053; Laminin_EGF; 5.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00180; EGF_Lam; 5.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; SSF49899; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 5.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186698};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1736       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012656926.
FT   DOMAIN       84    133       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      134    189       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      190    243       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      244    290       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      291    337       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      918   1115       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1127   1305       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1312   1478       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     1508   1668       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   REGION     1517   1538       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1L8G2U4}.
FT   COILED      435    455       {ECO:0000256|SAM:Coils}.
FT   COILED      552    586       {ECO:0000256|SAM:Coils}.
FT   COILED      650    670       {ECO:0000256|SAM:Coils}.
FT   COILED      779    813       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1517   1531       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1L8G2U4}.
FT   DISULFID    103    112       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    160    169       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    215    224       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    227    241       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    263    272       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    311    320       {ECO:0000256|PROSITE-ProRule:PRU00460}.
SQ   SEQUENCE   1736 AA;  192137 MW;  3339CBD0AD226505 CRC64;
     MGHFSRGYLI CLIMSLWRNL CHCSGSIEGS AFHLDSEGST SNPSDQDSGM VQLQHVVIPA
     RLVPLAQRCH LGFYYSVSGE CLPCNCNGNS LKCLDGSGEC LDCQRNTTGK HCERCPPGYL
     GNMVRGIPKS CLPCSCPLPF SPNNFALACG VKSGSMHCIC KDNYAGPNCE RCAPGYYGNP
     LLKGSTCKKC DCSGNSDPNL IFEDCNELTG QCNNCMRNTT GFNCELCAPG YYGDARVAKN
     CKECRCLKCG TERCNDVTGT CQCKPGVTGV FCDRCETGHY GYSSCLGCQK CMCSLASLDN
     NCDPETLQCN CKAGAGGLKC ERCKPGYWNY RPSGCQKCDC GGGPCNNITG ECLLEDPESL
     ANSDCSFDCD KCIWDLIDDL KIAASLADET KITALSISTG VMAHKHLNYI NSTLIHLTEM
     LEEKNNQSVF TDLITENAES KAEALQTNVN KLADKGNLAE MKESRFHKET METMKRAKLT
     AGQVNDIEDG IQELLGKLEY CESLHGDMSK ADRVTTLKQA EQILKDMADL NFMRTEILYE
     WQQVQNNTQS LLPNVNEKIA EYDNELADLY EAMEEARQHI NQTKEKNMAN IGKLQMSNIQ
     TVKLNKEVEN VSGSLTQSNI TLSGTHKLIS NISDITKNMT GHHAEVDGAY TGLKERLANL
     SRNVENIVEE AVNHSLTLQR EANGLSSNLK GIDANGFVQK AIDASNVHES IVNIIEAANE
     TSFIALGTAE SVNDASDGMD NQIKYQMTEN EKLWFQAKEL KEASDSSKDL RISETKQRVN
     AAALKNDALS DRLENAISQI EVHEDENTRK RLKKSKLVAE EALNITAMIT KVTNPMSKNA
     KIWTKEFSNT DFDASAYNKV VNSAGEAVRN LTEVVPLLLN KLHTVEYKWP TNNISSSILR
     IRELIAQTRS VASKVQVSMK FGGKSAVDVS LKTNVADLKA YSSISLFLNP VAHQEKPHDK
     FIMYFGNKNA TSDYMGLAIK SNNLVYVYNL GSGDVEIPLD SKPVNSWPGY FSLIKIERLG
     RHGKVLLTVP SPSSTAEEKF IKKGEATGKD SVLDLDPTSM VFYLGGVPPG FQLPASLNLP
     GFVGCLELAT VNDEVVSLYN FKNIYNLNTL TAPPCARNKL AFTQSRATSY FFDGTGYAVI
     RNIERRGRFT QVTRFDVEVR TPVDNALILL MVNGTKFFSL ELQDGYLRLQ YDFGFVRGPV
     LLEDSAKKFQ INDARYHEIS VIYHNSKKMI LVVDRRHVKS VDNEKTTIPF SDIYIGGAPS
     PILQSVKSHI AADISYKGCI KGFQFQKKDF NLLEEPETLG ISYGCPEESL MSRRAYFNGQ
     SFIASSQKLS PFDSFEGGFS FKTLQPSGLL LYHSEGADVF SVSMDKGSVV LRIKDIEVQS
     KNRKYSDGQN HFVVASVSPT RYQLLVDETD ASVQDRQKSE SSSPVARKFY FGGTPNGVSW
     ANFTGCISNA YFTRVDKDVE VEDFQKYTEK VQSSLYGCPV ESPPIALYQK NGKNSKKDKG
     KLKKSVGMEK KLASEAAKWS KEKEEDSEEL SQCSLSSRPK AGRQAHLYGG IANSRQEFNQ
     IPNGFNEKSE LFSHGRLTFM FNHGQQKIRI TSQEKYNDGL WHSVLCIREK NKGRLIINGL
     RVLEDSISAA DVMWTINSAY SFSGCLSNLQ MNGRSLTSPS QTFSVTPCFE GPMESGTYIS
     SEGGYVILDD SFSTGLTFEF ALEVRPRNNT GILIHFQNVN GEYLNLHMKQ GQVGKI
//
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