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Database: UniProt
Entry: S14L2_RAT
LinkDB: S14L2_RAT
Original site: S14L2_RAT 
ID   S14L2_RAT               Reviewed;         403 AA.
AC   Q99MS0;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=SEC14-like protein 2;
DE   AltName: Full=Alpha-tocopherol-associated protein;
DE            Short=TAP;
DE   AltName: Full=Squalene transfer protein;
DE   AltName: Full=Supernatant protein factor;
DE            Short=SPF;
GN   Name=Sec14l2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-51 AND 231-252.
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=11226224; DOI=10.1073/pnas.041620398;
RA   Shibata N., Arita M., Misaki Y., Dohmae N., Takio K., Ono T., Inoue K.,
RA   Arai H.;
RT   "Supernatant protein factor, which stimulates the conversion of squalene to
RT   lanosterol, is a cytosolic squalene transfer protein and enhances
RT   cholesterol biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:2244-2249(2001).
CC   -!- FUNCTION: Carrier protein. Binds to some hydrophobic molecules and
CC       promotes their transfer between the different cellular sites. Binds
CC       with high affinity to alpha-tocopherol. Also binds with a weaker
CC       affinity to other tocopherols and to tocotrienols. May have a
CC       transcriptional activatory activity via its association with alpha-
CC       tocopherol (By similarity). Probably recognizes and binds some squalene
CC       structure, suggesting that it may regulate cholesterol biosynthesis by
CC       increasing the transfer of squalene to a metabolic active pool in the
CC       cell. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Cytoplasmic in absence of alpha-tocopherol, and nuclear in
CC       presence of alpha-tocopherol. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q99MS0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99MS0-2; Sequence=Not described;
CC       Name=3;
CC         IsoId=Q99MS0-3; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Widely expressed. High expression in liver and
CC       small intestine.
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DR   EMBL; AF309558; AAK16405.1; -; mRNA.
DR   AlphaFoldDB; Q99MS0; -.
DR   SMR; Q99MS0; -.
DR   STRING; 10116.ENSRNOP00000006542; -.
DR   iPTMnet; Q99MS0; -.
DR   PhosphoSitePlus; Q99MS0; -.
DR   jPOST; Q99MS0; -.
DR   PaxDb; 10116-ENSRNOP00000006542; -.
DR   Ensembl; ENSRNOT00055051587; ENSRNOP00055042531; ENSRNOG00055029740. [Q99MS0-1]
DR   Ensembl; ENSRNOT00060038673; ENSRNOP00060031931; ENSRNOG00060022120. [Q99MS0-1]
DR   UCSC; RGD:621779; rat. [Q99MS0-1]
DR   AGR; RGD:621779; -.
DR   RGD; 621779; Sec14l2.
DR   eggNOG; KOG1471; Eukaryota.
DR   InParanoid; Q99MS0; -.
DR   PhylomeDB; Q99MS0; -.
DR   PRO; PR:Q99MS0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:RGD.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:RGD.
DR   GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IDA:RGD.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   PANTHER; PTHR23324; SEC14 RELATED PROTEIN; 1.
DR   PANTHER; PTHR23324:SF90; SEC14-LIKE PROTEIN 2; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Lipid-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transport.
FT   CHAIN           1..403
FT                   /note="SEC14-like protein 2"
FT                   /id="PRO_0000210757"
FT   DOMAIN          76..249
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   DOMAIN          275..383
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   MOD_RES         11
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99J08"
FT   MOD_RES         51
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99J08"
FT   MOD_RES         253
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99J08"
FT   MOD_RES         257
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99J08"
FT   MOD_RES         393
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99J08"
SQ   SEQUENCE   403 AA;  46166 MW;  413CC8BC4E3A45BD CRC64;
     MSGRVGDLSP KQEEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARSFDLQ KSEAMLRKHV
     EFRKQKDIDK IISWQPPEVI QQYLSGGRCG YDLDGCPVWY DIIGPLDAKG LLFSASKQDL
     LRTKMRDCEL LLQECTQQTA KLGKKIETIT MIYDCEGLGL KHLWKPAVEA YGEFLTMFEE
     NYPETLKRLF VVKAPKLFPV AYNLIKPFLS EDTRKKIMVL GANWKEVLLK HISPDQLPVE
     YGGTMTDPDG NPKCKSKINY GGDIPKQYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG
     CVLRWQFMSE GSDVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHMVPED GTLTCSEPGI
     YVLRFDNTYS FIHAKKVSFT VEVLLPDKAA EEKLNQQGAV TPK
//
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