STR3N_HUMAN
ID STR3N_HUMAN Reviewed; 234 AA.
AC O95772; A4D1X0;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=STARD3 N-terminal-like protein {ECO:0000303|PubMed:24105263};
DE AltName: Full=MLN64 N-terminal domain homolog;
GN Name=STARD3NL {ECO:0000303|PubMed:24105263, ECO:0000312|HGNC:HGNC:19169};
GN Synonyms=MENTHO {ECO:0000303|PubMed:12393907}; ORFNames=UNQ855/PRO1864;
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], TOPOLOGY, PHOSPHORYLATION, AND ALTERNATIVE
RP INITIATION.
RC TISSUE=Fetal brain;
RX PubMed=12393907; DOI=10.1074/jbc.m208290200;
RA Alpy F., Wendling C., Rio M.-C., Tomasetto C.;
RT "MENTHO, a MLN64 homologue devoid of the START domain.";
RL J. Biol. Chem. 277:50780-50787(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Kidney;
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 [8]
RP SUBUNIT, INTERACTION WITH STARD3NL, AND DOMAIN.
RX PubMed=15718238; DOI=10.1074/jbc.m500723200;
RA Alpy F., Latchumanan V.K., Kedinger V., Janoshazi A., Thiele C.,
RA Wendling C., Rio M.C., Tomasetto C.;
RT "Functional characterization of the MENTAL domain.";
RL J. Biol. Chem. 280:17945-17952(2005).
RN [9]
RP SUBUNIT, AND INTERACTION WITH STARD3.
RX PubMed=16709157; DOI=10.1042/bst0340343;
RA Alpy F., Tomasetto C.;
RT "MLN64 and MENTHO, two mediators of endosomal cholesterol transport.";
RL Biochem. Soc. Trans. 34:343-345(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-21, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAPA AND VAPB, AND FFAT
RP MOTIF.
RX PubMed=24105263; DOI=10.1242/jcs.139295;
RA Alpy F., Rousseau A., Schwab Y., Legueux F., Stoll I., Wendling C.,
RA Spiegelhalter C., Kessler P., Mathelin C., Rio M.C., Levine T.P.,
RA Tomasetto C.;
RT "STARD3 or STARD3NL and VAP form a novel molecular tether between late
RT endosomes and the ER.";
RL J. Cell Sci. 126:5500-5512(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-27 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MOSPD2, SUBCELLULAR
RP LOCATION, DOMAIN, FFAT MOTIF, AND MUTAGENESIS OF 209-TYR--LEU-234.
RX PubMed=29858488; DOI=10.15252/embr.201745453;
RA Di Mattia T., Wilhelm L.P., Ikhlef S., Wendling C., Spehner D., Nomine Y.,
RA Giordano F., Mathelin C., Drin G., Tomasetto C., Alpy F.;
RT "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum
RT membrane contact sites.";
RL EMBO Rep. 19:0-0(2018).
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 (PubMed:24105263). {ECO:0000269|PubMed:24105263}.
CC -!- SUBUNIT: Homodimer (PubMed:16709157). Interacts (via the MENTAL domain)
CC with STARD3NL (PubMed:16709157). Interacts (via FFAT motif) with VAPA.
CC Interacts (via FFAT motif) with VAPB (PubMed:24105263). Interacts (via
CC FFAT motif) with MOSPD2 (via MSP domain) (PubMed:29858488).
CC {ECO:0000269|PubMed:16709157, ECO:0000269|PubMed:24105263,
CC ECO:0000269|PubMed:29858488}.
CC -!- INTERACTION:
CC O95772; Q9UBK5: HCST; NbExp=3; IntAct=EBI-3916943, EBI-2801937;
CC O95772; Q8NHP6: MOSPD2; NbExp=5; IntAct=EBI-3916943, EBI-2812848;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:29858488}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to contact sites between
CC the endoplasmic reticulum and late endosomes: associates with the
CC endoplasmic reticulum membrane via interaction with VAPA, VAPB or
CC MOSPD2. {ECO:0000269|PubMed:24105263}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=O95772-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95772-2; Sequence=VSP_018819;
CC -!- DOMAIN: The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2.
CC {ECO:0000269|PubMed:29858488}.
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 (PubMed:15718238, PubMed:16709157).
CC {ECO:0000250|UniProtKB:Q14849, ECO:0000269|PubMed:15718238,
CC ECO:0000269|PubMed:16709157}.
CC -!- SIMILARITY: Belongs to the STARD3 family. {ECO:0000305}.
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DR EMBL; AJ492267; CAD37353.1; -; mRNA.
DR EMBL; AY358645; AAQ89008.1; -; mRNA.
DR EMBL; AK315404; BAG37796.1; -; mRNA.
DR EMBL; AC006033; AAS07552.1; -; Genomic_DNA.
DR EMBL; CH236951; EAL23983.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94088.1; -; Genomic_DNA.
DR EMBL; BC003074; AAH03074.1; -; mRNA.
DR EMBL; BC005959; AAH05959.1; -; mRNA.
DR CCDS; CCDS5455.1; -. [O95772-1]
DR RefSeq; NP_114405.1; NM_032016.3. [O95772-1]
DR RefSeq; XP_005249937.1; XM_005249880.1.
DR RefSeq; XP_011513874.1; XM_011515572.1. [O95772-1]
DR RefSeq; XP_016868181.1; XM_017012692.1.
DR RefSeq; XP_016868182.1; XM_017012693.1. [O95772-1]
DR RefSeq; XP_016868183.1; XM_017012694.1.
DR AlphaFoldDB; O95772; -.
DR BioGRID; 123815; 67.
DR IntAct; O95772; 8.
DR MINT; O95772; -.
DR STRING; 9606.ENSP00000009041; -.
DR iPTMnet; O95772; -.
DR PhosphoSitePlus; O95772; -.
DR SwissPalm; O95772; -.
DR BioMuta; STARD3NL; -.
DR CPTAC; CPTAC-1196; -.
DR CPTAC; CPTAC-1197; -.
DR EPD; O95772; -.
DR jPOST; O95772; -.
DR MassIVE; O95772; -.
DR MaxQB; O95772; -.
DR PaxDb; O95772; -.
DR PeptideAtlas; O95772; -.
DR PRIDE; O95772; -.
DR ProteomicsDB; 51038; -. [O95772-1]
DR ProteomicsDB; 51039; -. [O95772-2]
DR Antibodypedia; 3121; 31 antibodies from 16 providers.
DR DNASU; 83930; -.
DR Ensembl; ENST00000009041.12; ENSP00000009041.7; ENSG00000010270.14. [O95772-1]
DR Ensembl; ENST00000396013.5; ENSP00000379334.1; ENSG00000010270.14. [O95772-1]
DR GeneID; 83930; -.
DR KEGG; hsa:83930; -.
DR MANE-Select; ENST00000009041.12; ENSP00000009041.7; NM_032016.4; NP_114405.1.
DR UCSC; uc003tfr.4; human. [O95772-1]
DR CTD; 83930; -.
DR GeneCards; STARD3NL; -.
DR HGNC; HGNC:19169; STARD3NL.
DR HPA; ENSG00000010270; Low tissue specificity.
DR MIM; 611759; gene.
DR neXtProt; NX_O95772; -.
DR OpenTargets; ENSG00000010270; -.
DR PharmGKB; PA134990065; -.
DR VEuPathDB; HostDB:ENSG00000010270; -.
DR eggNOG; KOG3845; Eukaryota.
DR GeneTree; ENSGT00940000155476; -.
DR InParanoid; O95772; -.
DR OMA; HWWAVAI; -.
DR PhylomeDB; O95772; -.
DR TreeFam; TF313869; -.
DR PathwayCommons; O95772; -.
DR Reactome; R-HSA-196108; Pregnenolone biosynthesis.
DR SignaLink; O95772; -.
DR BioGRID-ORCS; 83930; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; STARD3NL; human.
DR GeneWiki; STARD3NL; -.
DR GenomeRNAi; 83930; -.
DR Pharos; O95772; Tbio.
DR PRO; PR:O95772; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O95772; protein.
DR Bgee; ENSG00000010270; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; O95772; baseline and differential.
DR Genevisible; O95772; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0044232; C:organelle membrane contact site; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0099044; P:vesicle tethering to endoplasmic reticulum; IDA:UniProtKB.
DR InterPro; IPR019498; MENTAL.
DR Pfam; PF10457; MENTAL; 1.
DR PROSITE; PS51439; MENTAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="STARD3 N-terminal-like protein"
FT /id="PRO_0000021666"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12393907"
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..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12393907"
FT DOMAIN 48..218
FT /note="MENTAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00770"
FT REGION 200..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 208..213
FT /note="FFAT"
FT /evidence="ECO:0000269|PubMed:24105263,
FT ECO:0000269|PubMed:29858488"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018819"
FT MUTAGEN 209..234
FT /note="Missing: Loss of interaction with MOSPD2."
FT /evidence="ECO:0000269|PubMed:29858488"
SQ SEQUENCE 234 AA; 26655 MW; AFB7DAE381983FB0 CRC64;
MNHLPEDMEN ALTGSQSSHA SLRNIHSINP TQLMARIESY EGREKKGISD VRRTFCLFVT
FDLLFVTLLW IIELNVNGGI ENTLEKEVMQ YDYYSSYFDI FLLAVFRFKV LILAYAVCRL
RHWWAIALTT AVTSAFLLAK VILSKLFSQG AFGYVLPIIS FILAWIETWF LDFKVLPQEA
EEENRLLIVQ DASERAALIP GGLSDGQFYS PPESEAGSEE AEEKQDSEKP LLEL
