ID B3RUG1_TRIAD Unreviewed; 1161 AA.
AC B3RUG1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV25807.1};
DE Flags: Fragment;
GN ORFNames=TRIADDRAFT_24524 {ECO:0000313|EMBL:EDV25807.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV25807.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV25807.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV25807.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; DS985244; EDV25807.1; -; Genomic_DNA.
DR RefSeq; XP_002111840.1; XM_002111804.1.
DR AlphaFoldDB; B3RUG1; -.
DR STRING; 10228.B3RUG1; -.
DR EnsemblMetazoa; TriadT24524; TriadP24524; TriadG24524.
DR GeneID; 6753053; -.
DR KEGG; tad:TRIADDRAFT_24524; -.
DR CTD; 6753053; -.
DR eggNOG; KOG0994; Eukaryota.
DR HOGENOM; CLU_001560_2_0_1; -.
DR InParanoid; B3RUG1; -.
DR OMA; PCANSHP; -.
DR OrthoDB; 90222at2759; -.
DR PhylomeDB; B3RUG1; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 11.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF444; -; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1161
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002798363"
FT DOMAIN 29..266
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 396..446
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 447..497
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 530..738
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 744..793
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 794..840
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 841..890
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 891..951
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 952..1003
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1004..1052
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1053..1100
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1101..1147
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 396..408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 398..415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 417..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 469..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 481..495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 766..775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 816..825
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 860..869
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 922..931
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 976..985
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1004..1016
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1006..1023
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1025..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1053..1065
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1055..1072
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1074..1083
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1101..1113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1103..1120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1122..1131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1161
FT /evidence="ECO:0000313|EMBL:EDV25807.1"
SQ SEQUENCE 1161 AA; 127848 MW; 7103030939A33ADF CRC64;
MRHIHSCNFL NYVNLISVKL TTVQCQDCLG KTCYPPSGEL LLGRGDQLTA TSTCGLNGPQ
RYCRVSDLDS EKKCFTCDSR PGRNETESHL VSNIVATSDT NRTWWQSENA VERVTLTLDF
EAEFQITHLI MTFLTFRPAA MIVSRSKDGG KNWRPYQYFA ENCATAFPNI RESINQRTFF
SDVICTRRYS QPKPASGGQV VFIAMPPGTT NDYGRSDPRV LDWITVTNIR FEFSKLQTLG
EAIGPRYPDN NEKYYYAISS LVVYGSCLCY GHASSCIPMP NTPPAKLNIR DMIHGKCSCQ
HFTSGTQCNV CLPEYNDQPW IAGYQENKGC SGCKCNNHTS TCSFSSTVYE RTNNASGSFC
TNCQDNTRGD QCNQCQPNYF QQANKSLDSP DVCARCDCDA RGTTNEPCNR LTGTCQCKSN
VMGNRCDSCK SSYYGLNDTN PLGCLPCNCY NDGTVDNTVC DVNSGQCSCE LNVDGRRCER
CKDTYWGLTS PSVQCRPCLC HPTGSYSLSC NDSTGLCPCR KNLVSPRCNQ VTANHYYSLM
DSIRFEAEEQ NASTVQTINH FYDYPYKLYS GTGYRIIQTN GIVRIVISVS YTFMYSLLVR
FEPTPGLNNF TITVDIKRPP SGVPINCDIP SSPLKFQNTS VDGAYITIPI CFGRDKNYIT
EIQYINNERV DVPLKLDSIV LWPSLTSLAS VELSTTLVKT LASAEAEYCS ELLYKPYNVS
DLSETCKEVM FTVSNILNDG GLVCDCNPTG TISGTACDKV GGQCRCKKNI FGRRCDKCLP
GAYGFGLPDG CRECKCDRQG STNFESCDAN TGQCNCKRNI VGLNCARCQY FYYGFPNCQR
CECYGHSASC DQRNGTCLNC LHNTAGPTCN QCRTGFVGTA TTGTPNDCVR CECPGGSSGN
QFSSTCYYRS TQSRTTIVCE NCTTGYTGNN CELCAPGYYG NPTSVGGRCL PCQCNNNINV
NEPGSCHNQT GECLKCLYNT GGPSCSQCRP GYYGKALTRT CRPCQCNEYG SVDGNCDPIT
GQCTCRSNVI GKTCDKCATG FWNITSGKGC QPCSCCRNNS LQANCDAVTG KCSCIKGYSG
DKCCDCEDGF WGNPSTTCYA CNCNKMGSLS TECDRKTGQC YCIAAAGGFR CDRCADGYQG
TFPSCRRCHV CYFDWNKRIT D
//
