ID B3RQ21_TRIAD Unreviewed; 518 AA.
AC B3RQ21;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=SMP-LTD domain-containing protein {ECO:0000259|PROSITE:PS51847};
GN ORFNames=TRIADDRAFT_21124 {ECO:0000313|EMBL:EDV28278.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28278.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28278.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28278.1,
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).
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DR EMBL; DS985242; EDV28278.1; -; Genomic_DNA.
DR RefSeq; XP_002110112.1; XM_002110076.1.
DR AlphaFoldDB; B3RQ21; -.
DR STRING; 10228.B3RQ21; -.
DR EnsemblMetazoa; TriadT21124; TriadP21124; TriadG21124.
DR GeneID; 6750794; -.
DR KEGG; tad:TRIADDRAFT_21124; -.
DR CTD; 6750794; -.
DR eggNOG; KOG2238; Eukaryota.
DR HOGENOM; CLU_015992_0_0_1; -.
DR InParanoid; B3RQ21; -.
DR OMA; LGTVKWK; -.
DR OrthoDB; 25570at2759; -.
DR PhylomeDB; B3RQ21; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd21675; SMP_TEX2; 1.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR13466:SF0; SMP-LTD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13466; TEX2 PROTEIN-RELATED; 1.
DR Pfam; PF10296; MMM1; 1.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT DOMAIN 226..506
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 161..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 58830 MW; A34834770885F26A CRC64;
MYGKRKYDQD QHYKTDLRCI YARLDGSVLR LSKPQSDDLT IPFKPEKWNV SFVNQKLLDI
TNAKIQLIPK TLSKNKLWSK KYPICITLAE GKSFSGAPTA AVDKSPLEYQ PASGKVQLPT
VDPSPNIDSE KDRSFYLFAT TSHDKEYWFY RLQYGTESKK EETLPIDKEP KVYPPSHPNV
QPNRSKTFAE MQAIYYSRYM AKLILQVDNK PKSKQQQPAA GKNPVETSVV SWLNALLGRA
FFDFWREKYW SDKMVNIIQR RISKLNRPNY IKELIVTDLD LGGSLPAIRG ASSPTLDERG
LWIDLDVSYH GSFTIALETS LNITRQKPDG EMEVTDPKKE TDPSKNDLIF TLQGLDKSDS
ESSDDEADDP TLEKQSSSSS IGSSQHNGNS RWSRFIKKVG KSKIVQKATN SRLAQKAAER
VSNIPIILAV EIQSVTGILA LNIPPPPSDR LWYGFRGNPT VLMSVRPKLG ERKVRLTNIT
DWIEKKLRHE IKETIVLPHM IDYKIALMGN TMTEIAIS
//
