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 03-AUG-2022, entry version 123.
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; Q99MS0; -.
DR PRIDE; Q99MS0; -.
DR UCSC; RGD:621779; rat. [Q99MS0-1]
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; IDA:RGD.
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; -; 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 Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 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
