STAR4_HUMAN
ID STAR4_HUMAN Reviewed; 205 AA.
AC Q96DR4; Q86TN9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=StAR-related lipid transfer protein 4;
DE AltName: Full=START domain-containing protein 4;
DE Short=StARD4;
GN Name=STARD4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=12011452; DOI=10.1073/pnas.052143799;
RA Soccio R.E., Adams R.M., Romanowski M.J., Sehayek E., Burley S.K.,
RA Breslow J.L.;
RT "The cholesterol-regulated StarD4 gene encodes a StAR-related lipid
RT transfer protein with two closely related homologues, StarD5 and StarD6.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6943-6948(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=18403318; DOI=10.1194/jlr.m700537-jlr200;
RA Rodriguez-Agudo D., Ren S., Wong E., Marques D., Redford K., Gil G.,
RA Hylemon P., Pandak W.M.;
RT "Intracellular cholesterol transporter StarD4 binds free cholesterol and
RT increases cholesteryl ester formation.";
RL J. Lipid Res. 49:1409-1419(2008).
CC -!- FUNCTION: Involved in the intracellular transport of cholesterol. Binds
CC cholesterol or other sterols. {ECO:0000269|PubMed:18403318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:18403318};
CC -!- INTERACTION:
CC Q96DR4; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-17217258, EBI-11522760;
CC Q96DR4; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-17217258, EBI-714543;
CC Q96DR4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-17217258, EBI-10175300;
CC Q96DR4; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-17217258, EBI-11110431;
CC Q96DR4; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-17217258, EBI-3923617;
CC Q96DR4; P08247: SYP; NbExp=3; IntAct=EBI-17217258, EBI-9071725;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DR4-2; Sequence=VSP_057170;
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DR EMBL; AF480299; AAL87129.1; -; mRNA.
DR EMBL; AK054566; BAB70759.1; -; mRNA.
DR EMBL; AC011422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW49029.1; -; Genomic_DNA.
DR EMBL; BC042956; AAH42956.1; -; mRNA.
DR CCDS; CCDS4104.1; -. [Q96DR4-1]
DR CCDS; CCDS78046.1; -. [Q96DR4-2]
DR RefSeq; NP_001294985.1; NM_001308056.1. [Q96DR4-1]
DR RefSeq; NP_001294986.1; NM_001308057.1. [Q96DR4-2]
DR RefSeq; NP_001294987.1; NM_001308058.1. [Q96DR4-2]
DR RefSeq; NP_001294988.1; NM_001308059.1.
DR RefSeq; NP_001294989.1; NM_001308060.1.
DR RefSeq; NP_001294990.1; NM_001308061.1.
DR RefSeq; NP_631903.1; NM_139164.2. [Q96DR4-1]
DR PDB; 6L1D; X-ray; 1.95 A; A/B=2-205.
DR PDB; 6L1M; X-ray; 1.70 A; A=2-205.
DR PDBsum; 6L1D; -.
DR PDBsum; 6L1M; -.
DR AlphaFoldDB; Q96DR4; -.
DR SMR; Q96DR4; -.
DR BioGRID; 126398; 6.
DR IntAct; Q96DR4; 6.
DR STRING; 9606.ENSP00000296632; -.
DR SwissLipids; SLP:000000718; -.
DR SwissLipids; SLP:000000719; -.
DR iPTMnet; Q96DR4; -.
DR PhosphoSitePlus; Q96DR4; -.
DR BioMuta; STARD4; -.
DR DMDM; 25091316; -.
DR EPD; Q96DR4; -.
DR jPOST; Q96DR4; -.
DR MassIVE; Q96DR4; -.
DR MaxQB; Q96DR4; -.
DR PaxDb; Q96DR4; -.
DR PeptideAtlas; Q96DR4; -.
DR PRIDE; Q96DR4; -.
DR ProteomicsDB; 69718; -.
DR ProteomicsDB; 76305; -. [Q96DR4-1]
DR Antibodypedia; 25323; 106 antibodies from 16 providers.
DR DNASU; 134429; -.
DR Ensembl; ENST00000296632.8; ENSP00000296632.3; ENSG00000164211.13. [Q96DR4-1]
DR Ensembl; ENST00000502322.5; ENSP00000427639.1; ENSG00000164211.13. [Q96DR4-2]
DR Ensembl; ENST00000505803.5; ENSP00000427478.2; ENSG00000164211.13. [Q96DR4-1]
DR GeneID; 134429; -.
DR KEGG; hsa:134429; -.
DR MANE-Select; ENST00000296632.8; ENSP00000296632.3; NM_139164.3; NP_631903.1.
DR UCSC; uc003kph.2; human. [Q96DR4-1]
DR CTD; 134429; -.
DR GeneCards; STARD4; -.
DR HGNC; HGNC:18058; STARD4.
DR HPA; ENSG00000164211; Low tissue specificity.
DR MIM; 607049; gene.
DR neXtProt; NX_Q96DR4; -.
DR OpenTargets; ENSG00000164211; -.
DR PharmGKB; PA38284; -.
DR VEuPathDB; HostDB:ENSG00000164211; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000159243; -.
DR HOGENOM; CLU_093200_0_0_1; -.
DR InParanoid; Q96DR4; -.
DR OMA; TLILYHN; -.
DR OrthoDB; 1469639at2759; -.
DR PhylomeDB; Q96DR4; -.
DR PathwayCommons; Q96DR4; -.
DR Reactome; R-HSA-196108; Pregnenolone biosynthesis.
DR SignaLink; Q96DR4; -.
DR BioGRID-ORCS; 134429; 28 hits in 1081 CRISPR screens.
DR GeneWiki; STARD4; -.
DR GenomeRNAi; 134429; -.
DR Pharos; Q96DR4; Tbio.
DR PRO; PR:Q96DR4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96DR4; protein.
DR Bgee; ENSG00000164211; Expressed in adrenal tissue and 146 other tissues.
DR ExpressionAtlas; Q96DR4; baseline and differential.
DR Genevisible; Q96DR4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:BHF-UCL.
DR GO; GO:0070508; P:cholesterol import; IDA:BHF-UCL.
DR GO; GO:0010879; P:cholesterol transport involved in cholesterol storage; IDA:BHF-UCL.
DR GO; GO:0032367; P:intracellular cholesterol transport; IDA:BHF-UCL.
DR GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IDA:BHF-UCL.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR042555; StarD4.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR47006; PTHR47006; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lipid transport; Lipid-binding;
KW Reference proteome; Transport.
FT CHAIN 1..205
FT /note="StAR-related lipid transfer protein 4"
FT /id="PRO_0000220667"
FT DOMAIN 1..205
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT VAR_SEQ 134..204
FT /note="ISLDWDEKRPEFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGMIPQSA
FT VDTAMASTLTNFYGDLRKA -> NNLNMLCFFSVWFKYLCFLGWMSLS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057170"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:6L1M"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 46..61
FT /evidence="ECO:0007829|PDB:6L1M"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6L1M"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:6L1M"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:6L1D"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6L1M"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:6L1M"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:6L1M"
SQ SEQUENCE 205 AA; 23517 MW; 59A8D4B95BFAE27F CRC64;
MEGLSDVASF ATKLKNTLIQ YHSIEEDKWR VAKKTKDVTV WRKPSEEFNG YLYKAQGVID
DLVYSIIDHI RPGPCRLDWD SLMTSLDILE NFEENCCVMR YTTAGQLWNI ISPREFVDFS
YTVGYKEGLL SCGISLDWDE KRPEFVRGYN HPCGWFCVPL KDNPNQSLLT GYIQTDLRGM
IPQSAVDTAM ASTLTNFYGD LRKAL
