STR3N_MOUSE
ID STR3N_MOUSE Reviewed; 235 AA.
AC Q9DCI3; Q3U8Q7; Q99J63; Q9D356;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=STARD3 N-terminal-like protein {ECO:0000250|UniProtKB:O95772};
DE AltName: Full=MLN64 N-terminal domain homolog {ECO:0000250|UniProtKB:O95772};
GN Name=Stard3nl {ECO:0000312|MGI:MGI:1923455};
GN Synonyms=Mentho {ECO:0000250|UniProtKB:O95772};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Tethering protein that creates contact site between the
CC endoplasmic reticulum and late endosomes: localizes to late endosome
CC membranes and contacts the endoplasmic reticulum via interaction with
CC VAPA and VAPB. {ECO:0000250|UniProtKB:O95772}.
CC -!- SUBUNIT: Homodimer. Interacts (via the MENTAL domain) with STARD3NL.
CC Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with
CC VAPB. Interacts (via FFAT motif) with MOSPD2 (via MSP domain).
CC {ECO:0000250|UniProtKB:O95772}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:O95772}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic
CC reticulum and late endosomes: associates with the endoplasmic reticulum
CC membrane via interaction with VAPA, VAPB or MOSPD2.
CC {ECO:0000250|UniProtKB:O95772}.
CC -!- DOMAIN: The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2.
CC {ECO:0000250|UniProtKB:O95772}.
CC -!- DOMAIN: The MENTAL domain anchors the protein in endosome membranes and
CC exposes the START domain in the cytosol (By similarity). It binds
CC cholesterol and mediates homotypic as well as heterotypic interactions
CC between STARD3 and STARD3NL (By similarity).
CC {ECO:0000250|UniProtKB:O95772, ECO:0000250|UniProtKB:Q14849}.
CC -!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
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DR EMBL; AK002760; BAB22337.1; -; mRNA.
DR EMBL; AK152116; BAE30960.1; -; mRNA.
DR EMBL; BC003334; AAH03334.1; -; mRNA.
DR CCDS; CCDS26259.1; -.
DR RefSeq; NP_077232.2; NM_024270.3.
DR AlphaFoldDB; Q9DCI3; -.
DR SMR; Q9DCI3; -.
DR BioGRID; 218022; 1.
DR STRING; 10090.ENSMUSP00000037991; -.
DR iPTMnet; Q9DCI3; -.
DR PhosphoSitePlus; Q9DCI3; -.
DR SwissPalm; Q9DCI3; -.
DR jPOST; Q9DCI3; -.
DR MaxQB; Q9DCI3; -.
DR PaxDb; Q9DCI3; -.
DR PRIDE; Q9DCI3; -.
DR ProteomicsDB; 258648; -.
DR Antibodypedia; 3121; 31 antibodies from 16 providers.
DR DNASU; 76205; -.
DR Ensembl; ENSMUST00000039694; ENSMUSP00000037991; ENSMUSG00000003062.
DR Ensembl; ENSMUST00000197565; ENSMUSP00000152747; ENSMUSG00000003062.
DR GeneID; 76205; -.
DR KEGG; mmu:76205; -.
DR UCSC; uc007ppa.1; mouse.
DR CTD; 83930; -.
DR MGI; MGI:1923455; Stard3nl.
DR VEuPathDB; HostDB:ENSMUSG00000003062; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000155476; -.
DR HOGENOM; CLU_102230_0_0_1; -.
DR InParanoid; Q9DCI3; -.
DR OMA; HWWAVAI; -.
DR PhylomeDB; Q9DCI3; -.
DR TreeFam; TF313869; -.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR BioGRID-ORCS; 76205; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Stard3nl; mouse.
DR PRO; PR:Q9DCI3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9DCI3; protein.
DR Bgee; ENSMUSG00000003062; Expressed in basioccipital bone and 287 other tissues.
DR ExpressionAtlas; Q9DCI3; baseline and differential.
DR Genevisible; Q9DCI3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; ISS:UniProtKB.
DR InterPro; IPR019498; MENTAL.
DR Pfam; PF10457; MENTAL; 1.
DR PROSITE; PS51439; MENTAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..235
FT /note="STARD3 N-terminal-like protein"
FT /id="PRO_0000096420"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O95772"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 75..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 119..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 144..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT TOPO_DOM 172..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O95772"
FT DOMAIN 48..218
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 208..213
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:O95772"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95772"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95772"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95772"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 32..33
FT /note="QL -> HS (in Ref. 1; BAB22337)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="R -> G (in Ref. 2; AAH03334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 26811 MW; F251725390CB1503 CRC64;
MNHLPEHMEN TLTGSQSSHA SLRDIHSINP AQLMARIESY EGREKKGISD VRRTFCLFVT
FDLLFVTLLW IIELNVNGGI ENTLKKEVIH YDYYSSYFDI FLLAVFRFKV LILGYAVCRL
RHWWAIALTT AVTSAFLLAK VILSKLFSQG AFGYVLPIIS FILAWIETWF LDFKVLPQEA
EEENRLLLVQ DASERAALIP AGLSDGQFYS PPESEAGSEE EAEEKQESEK PLLEL
