LITAF_HUMAN
ID LITAF_HUMAN Reviewed; 161 AA.
AC Q99732; D3DUG1; G5E9K0; Q05DW0; Q9C0L6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha factor {ECO:0000303|PubMed:10200294};
DE Short=LPS-induced TNF-alpha factor {ECO:0000303|PubMed:10200294};
DE AltName: Full=Small integral membrane protein of lysosome/late endosome {ECO:0000303|PubMed:11274176};
DE AltName: Full=p53-induced gene 7 protein {ECO:0000303|PubMed:11274176};
GN Name=LITAF;
GN Synonyms=PIG7 {ECO:0000303|PubMed:11274176, ECO:0000303|PubMed:15197774},
GN SIMPLE {ECO:0000303|PubMed:11274176};
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 2), AND INDUCTION BY TP53.
RC TISSUE=Colon cancer;
RX PubMed=9305847; DOI=10.1038/38525;
RA Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
RT "A model for p53-induced apoptosis.";
RL Nature 389:300-306(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Monocyte;
RX PubMed=10200294; DOI=10.1073/pnas.96.8.4518;
RA Myokai F., Takashiba S., Lebo R., Amar S.;
RT "A novel lipopolysaccharide-induced transcription factor regulating tumor
RT necrosis factor alpha gene expression: molecular cloning, sequencing,
RT characterization, and chromosomal assignment.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4518-4523(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Monocyte;
RX PubMed=11274176; DOI=10.1074/jbc.m011660200;
RA Moriwaki Y., Begum N.A., Kobayashi M., Matsumoto M., Toyoshima K., Seya T.;
RT "Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex
RT induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing
RT link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and
RT estrogen-inducible gene, EET-1.";
RL J. Biol. Chem. 276:23065-23076(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hair follicle dermal papilla;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, Pancreas, PNS, and Skin;
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 [9]
RP INTERACTION WITH WWOX, DOMAIN, AND MUTAGENESIS OF TYR-23 AND TYR-61.
RX PubMed=15064722; DOI=10.1038/sj.onc.1207680;
RA Ludes-Meyers J.H., Kil H., Bednarek A.K., Drake J., Bedford M.T.,
RA Aldaz C.M.;
RT "WWOX binds the specific proline-rich ligand PPXY: identification of
RT candidate interacting proteins.";
RL Oncogene 23:5049-5055(2004).
RN [10]
RP INTERACTION WITH NEDD4 AND TSG101, CHARACTERIZATION OF VARIANTS CMT1C
RP SER-112; ASN-115 AND GLY-116, AND MUTAGENESIS OF 17-PRO--ALA-19 AND TYR-23.
RX PubMed=16118794; DOI=10.1002/jnr.20628;
RA Shirk A.J., Anderson S.K., Hashemi S.H., Chance P.F., Bennett C.L.;
RT "SIMPLE interacts with NEDD4 and TSG101: evidence for a role in lysosomal
RT sorting and implications for Charcot-Marie-Tooth disease.";
RL J. Neurosci. Res. 82:43-50(2005).
RN [11]
RP FUNCTION, INTERACTION WITH STAT6, SUBCELLULAR LOCATION, AND INDUCTION BY
RP LIPOPOLYSACCHARIDE.
RX PubMed=15793005; DOI=10.1073/pnas.0501159102;
RA Tang X., Marciano D.L., Leeman S.E., Amar S.;
RT "LPS induces the interaction of a transcription factor, LPS-induced TNF-
RT alpha factor, and STAT6(B) with effects on multiple cytokines.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5132-5137(2005).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16954198; DOI=10.1073/pnas.0605988103;
RA Tang X., Metzger D., Leeman S., Amar S.;
RT "LPS-induced TNF-alpha factor (LITAF)-deficient mice express reduced LPS-
RT induced cytokine: Evidence for LITAF-dependent LPS signaling pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13777-13782(2006).
RN [13]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-135, AND CHARACTERIZATION OF
RP VARIANT CMT1C GLY-116.
RX PubMed=21896645; DOI=10.1242/jcs.087114;
RA Lee S.M., Olzmann J.A., Chin L.S., Li L.;
RT "Mutations associated with Charcot-Marie-Tooth disease cause SIMPLE protein
RT mislocalization and degradation by the proteasome and aggresome-autophagy
RT pathways.";
RL J. Cell Sci. 124:3319-3331(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH TSG101; STAM AND
RP HGS, PHOSPHORYLATION, MUTAGENESIS OF 17-PRO--PRO-20 AND PRO-135, AND
RP CHARACTERIZATION OF VARIANT CMT1C GLY-116.
RX PubMed=23166352; DOI=10.1083/jcb.201204137;
RA Lee S.M., Chin L.S., Li L.;
RT "Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT
RT machinery in endosomal trafficking.";
RL J. Cell Biol. 199:799-816(2012).
RN [15]
RP 3D-STRUCTURE MODELING, NMR SECONDARY STRUCTURE ANALYSIS, SUBCELLULAR
RP LOCATION, TOPOLOGY, ZINC-BINDING, SUBUNIT, INTERACTION WITH NEDD4, DOMAIN,
RP AND MUTAGENESIS OF TYR-23; TYR-61 AND VAL-144.
RX PubMed=27927196; DOI=10.1186/s12915-016-0332-8;
RA Ho A.K., Wagstaff J.L., Manna P.T., Wartosch L., Qamar S., Garman E.F.,
RA Freund S.M., Roberts R.C.;
RT "The topology, structure and PE interaction of LITAF underpin a Charcot-
RT Marie-Tooth disease type 1C.";
RL BMC Biol. 14:109-109(2016).
RN [16]
RP ZINC-BINDING, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYS-96 AND
RP CYS-148, AND DOMAIN.
RX PubMed=27582497; DOI=10.1042/bcj20160657;
RA Qin W., Wunderley L., Barrett A.L., High S., Woodman P.G.;
RT "The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic
RT membrane protein.";
RL Biochem. J. 473:3965-3978(2016).
RN [17]
RP VARIANTS CMT1C SER-112; ASN-115 AND GLY-116.
RX PubMed=12525712; DOI=10.1212/wnl.60.1.22;
RA Street V.A., Bennett C.L., Goldy J.D., Shirk A.J., Kleopa K.A.,
RA Tempel B.L., Lipe H.P., Scherer S.S., Bird T.D., Chance P.F.;
RT "Mutation of a putative protein degradation gene LITAF/SIMPLE in Charcot-
RT Marie-Tooth disease 1C.";
RL Neurology 60:22-26(2003).
RN [18]
RP VARIANT EMPD HIS-23.
RX PubMed=15197774; DOI=10.1002/ijc.20251;
RA Matsumura Y., Matsumura Y., Nishigori C., Horio T., Miyachi Y.;
RT "PIG7/LITAF gene mutation and overexpression of its gene product in
RT extramammary Paget's disease.";
RL Int. J. Cancer 111:218-223(2004).
RN [19]
RP VARIANT CMT1C SER-112, AND VARIANT VAL-92.
RX PubMed=15786462; DOI=10.1002/ana.20434;
RA Meggouh F., de Visser M., Arts W.F.M., De Coo R.I.F.M., van Schaik I.N.,
RA Baas F.;
RT "Early onset neuropathy in a compound form of Charcot-Marie-Tooth
RT disease.";
RL Ann. Neurol. 57:589-591(2005).
RN [20]
RP VARIANTS CMT1C MET-49; SER-112 AND VAL-122, VARIANT VAL-92, AND PUTATIVE
RP FUNCTION.
RX PubMed=15776429; DOI=10.1002/humu.20153;
RA Saifi G.M., Szigeti K., Wiszniewski W., Shy M.E., Krajewski K.,
RA Hausmanowa-Petrusewicz I., Kochanski A., Reeser S., Mancias P., Butler I.,
RA Lupski J.R.;
RT "SIMPLE mutations in Charcot-Marie-Tooth disease and the potential role of
RT its protein product in protein degradation.";
RL Hum. Mutat. 25:372-383(2005).
RN [21]
RP VARIANT CMT1C SER-112.
RX PubMed=24604904; DOI=10.1136/jnnp-2013-306740;
RA Klein C.J., Middha S., Duan X., Wu Y., Litchy W.J., Gu W., Dyck P.J.,
RA Gavrilova R.H., Smith D.I., Kocher J.P., Dyck P.J.;
RT "Application of whole exome sequencing in undiagnosed inherited
RT polyneuropathies.";
RL J. Neurol. Neurosurg. Psych. 85:1265-1272(2014).
CC -!- FUNCTION: Plays a role in endosomal protein trafficking and in
CC targeting proteins for lysosomal degradation (PubMed:23166352). Plays a
CC role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation,
CC and thereby helps down-regulate downstream signaling cascades
CC (PubMed:23166352). Helps recruit the ESCRT complex components TSG101,
CC HGS and STAM to cytoplasmic membranes (PubMed:23166352). Probably plays
CC a role in regulating protein degradation via its interaction with NEDD4
CC (PubMed:15776429). May also contribute to the regulation of gene
CC expression in the nucleus (PubMed:10200294, PubMed:15793005). Binds DNA
CC (in vitro) and may play a synergistic role with STAT6 in the nucleus in
CC regulating the expression of various cytokines (PubMed:15793005). May
CC regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5,
CC CXCL1, IL1A and IL10 (PubMed:10200294, PubMed:15793005).
CC {ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:23166352,
CC ECO:0000303|PubMed:15776429, ECO:0000305|PubMed:10200294}.
CC -!- SUBUNIT: Monomer (PubMed:27927196). Interacts with NEDD4
CC (PubMed:16118794, PubMed:27927196). Interacts (via PSAP motif) with
CC TSG101, a component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) (PubMed:16118794). Interacts with WWOX
CC (PubMed:15064722). Interacts with STAM, a component of the ESCRT-0
CC complex; the interaction is direct (PubMed:23166352). Identified in a
CC complex with STAM and HGS; within this complex, interacts directly with
CC STAM, but not with HGS (PubMed:23166352). Interacts with STAT6
CC (PubMed:15793005). {ECO:0000269|PubMed:15064722,
CC ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:23166352,
CC ECO:0000269|PubMed:27927196, ECO:0000305|PubMed:15793005}.
CC -!- INTERACTION:
CC Q99732; Q9UKA4: AKAP11; NbExp=3; IntAct=EBI-725647, EBI-1049491;
CC Q99732; Q03989: ARID5A; NbExp=3; IntAct=EBI-725647, EBI-948603;
CC Q99732; Q9BVU5: ARL17; NbExp=3; IntAct=EBI-725647, EBI-25857117;
CC Q99732; O95817: BAG3; NbExp=7; IntAct=EBI-725647, EBI-747185;
CC Q99732; P80723: BASP1; NbExp=3; IntAct=EBI-725647, EBI-358583;
CC Q99732; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-725647, EBI-739580;
CC Q99732; Q9HC96: CAPN10; NbExp=3; IntAct=EBI-725647, EBI-3915761;
CC Q99732; P83916: CBX1; NbExp=3; IntAct=EBI-725647, EBI-78129;
CC Q99732; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-725647, EBI-1773949;
CC Q99732; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-725647, EBI-745535;
CC Q99732; Q92828: CORO2A; NbExp=3; IntAct=EBI-725647, EBI-2835660;
CC Q99732; Q02930-3: CREB5; NbExp=3; IntAct=EBI-725647, EBI-10192698;
CC Q99732; Q9UN19: DAPP1; NbExp=3; IntAct=EBI-725647, EBI-3918199;
CC Q99732; Q15038: DAZAP2; NbExp=5; IntAct=EBI-725647, EBI-724310;
CC Q99732; Q9NR30: DDX21; NbExp=3; IntAct=EBI-725647, EBI-357942;
CC Q99732; Q92608-2: DOCK2; NbExp=3; IntAct=EBI-725647, EBI-25875570;
CC Q99732; Q9Y6I3-3: EPN1; NbExp=3; IntAct=EBI-725647, EBI-12026538;
CC Q99732; O95208-2: EPN2; NbExp=5; IntAct=EBI-725647, EBI-12135243;
CC Q99732; I6L9I8: EPN3; NbExp=5; IntAct=EBI-725647, EBI-12866582;
CC Q99732; Q9NZ52-2: GGA3; NbExp=3; IntAct=EBI-725647, EBI-12075758;
CC Q99732; O14964: HGS; NbExp=8; IntAct=EBI-725647, EBI-740220;
CC Q99732; O00291: HIP1; NbExp=6; IntAct=EBI-725647, EBI-473886;
CC Q99732; P37235: HPCAL1; NbExp=4; IntAct=EBI-725647, EBI-749311;
CC Q99732; Q9UM19: HPCAL4; NbExp=6; IntAct=EBI-725647, EBI-744820;
CC Q99732; Q96T52-2: IMMP2L; NbExp=3; IntAct=EBI-725647, EBI-25907627;
CC Q99732; Q9NZI2-2: KCNIP1; NbExp=3; IntAct=EBI-725647, EBI-22452746;
CC Q99732; Q6PIL6: KCNIP4; NbExp=3; IntAct=EBI-725647, EBI-1051469;
CC Q99732; P13473-2: LAMP2; NbExp=3; IntAct=EBI-725647, EBI-21591415;
CC Q99732; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-725647, EBI-10274069;
CC Q99732; Q99732: LITAF; NbExp=2; IntAct=EBI-725647, EBI-725647;
CC Q99732; Q9BYD3: MRPL4; NbExp=3; IntAct=EBI-725647, EBI-721368;
CC Q99732; O75113: N4BP1; NbExp=3; IntAct=EBI-725647, EBI-5278391;
CC Q99732; P61601: NCALD; NbExp=5; IntAct=EBI-725647, EBI-749635;
CC Q99732; P46934: NEDD4; NbExp=7; IntAct=EBI-725647, EBI-726944;
CC Q99732; Q96CV9: OPTN; NbExp=3; IntAct=EBI-725647, EBI-748974;
CC Q99732; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-725647, EBI-9091423;
CC Q99732; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-725647, EBI-1389308;
CC Q99732; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-725647, EBI-438710;
CC Q99732; Q86WH2: RASSF3; NbExp=4; IntAct=EBI-725647, EBI-2845202;
CC Q99732; Q96HR9: REEP6; NbExp=8; IntAct=EBI-725647, EBI-750345;
CC Q99732; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-725647, EBI-14065960;
CC Q99732; Q8N8N0: RNF152; NbExp=3; IntAct=EBI-725647, EBI-2129725;
CC Q99732; Q96D59: RNF183; NbExp=3; IntAct=EBI-725647, EBI-743938;
CC Q99732; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-725647, EBI-751555;
CC Q99732; P62979: RPS27A; NbExp=3; IntAct=EBI-725647, EBI-357375;
CC Q99732; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-725647, EBI-11528848;
CC Q99732; Q99717: SMAD5; NbExp=3; IntAct=EBI-725647, EBI-6391136;
CC Q99732; Q9C0H9-4: SRCIN1; NbExp=3; IntAct=EBI-725647, EBI-25907611;
CC Q99732; O75886: STAM2; NbExp=11; IntAct=EBI-725647, EBI-373258;
CC Q99732; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-725647, EBI-529518;
CC Q99732; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-725647, EBI-2800645;
CC Q99732; Q15025: TNIP1; NbExp=3; IntAct=EBI-725647, EBI-357849;
CC Q99732; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-725647, EBI-2509913;
CC Q99732; O60784-2: TOM1; NbExp=3; IntAct=EBI-725647, EBI-12117154;
CC Q99732; Q99816: TSG101; NbExp=3; IntAct=EBI-725647, EBI-346882;
CC Q99732; P62987: UBA52; NbExp=3; IntAct=EBI-725647, EBI-357304;
CC Q99732; O14933: UBE2L6; NbExp=3; IntAct=EBI-725647, EBI-2129974;
CC Q99732; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-725647, EBI-741480;
CC Q99732; Q9UMX0-2: UBQLN1; NbExp=7; IntAct=EBI-725647, EBI-10173939;
CC Q99732; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-725647, EBI-947187;
CC Q99732; O95231: VENTX; NbExp=3; IntAct=EBI-725647, EBI-10191303;
CC Q99732; O15195-2: VILL; NbExp=3; IntAct=EBI-725647, EBI-21845957;
CC Q99732; P62760: VSNL1; NbExp=3; IntAct=EBI-725647, EBI-740943;
CC Q99732; Q9NZC7: WWOX; NbExp=5; IntAct=EBI-725647, EBI-4320739;
CC Q99732; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-725647, EBI-12040603;
CC Q99732; O00308: WWP2; NbExp=3; IntAct=EBI-725647, EBI-743923;
CC Q99732; P46937: YAP1; NbExp=2; IntAct=EBI-725647, EBI-1044059;
CC Q99732; Q15915: ZIC1; NbExp=3; IntAct=EBI-725647, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15793005}. Nucleus
CC {ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:16954198}. Lysosome
CC membrane {ECO:0000269|PubMed:11274176, ECO:0000269|PubMed:27582497};
CC Peripheral membrane protein {ECO:0000269|PubMed:11274176}; Cytoplasmic
CC side {ECO:0000269|PubMed:11274176}. Early endosome membrane
CC {ECO:0000269|PubMed:21896645, ECO:0000269|PubMed:23166352,
CC ECO:0000269|PubMed:27582497}. Late endosome membrane
CC {ECO:0000269|PubMed:27582497}. Endosome membrane
CC {ECO:0000269|PubMed:27927196}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27927196}; Cytoplasmic side
CC {ECO:0000269|PubMed:27927196}. Cell membrane
CC {ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:27582497}; Peripheral
CC membrane protein {ECO:0000269|PubMed:27582497}; Cytoplasmic side
CC {ECO:0000269|PubMed:27582497}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16118794}. Note=Associated with membranes of
CC lysosomes, early and late endosomes (PubMed:11274176, PubMed:27927196,
CC PubMed:27582497). Can translocate from the cytoplasm into the nucleus
CC (PubMed:15793005). Detected at Schmidt-Lanterman incisures and in nodal
CC regions of myelinating Schwann cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9JLJ0, ECO:0000269|PubMed:11274176,
CC ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:27582497,
CC ECO:0000269|PubMed:27927196}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99732-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99732-2; Sequence=VSP_016461;
CC Name=3;
CC IsoId=Q99732-3; Sequence=VSP_045701;
CC -!- TISSUE SPECIFICITY: Ubiquitously and abundantly expressed. Expressed
CC predominantly in the placenta, peripheral blood leukocytes, lymph nodes
CC and spleen. {ECO:0000269|PubMed:10200294, ECO:0000269|PubMed:11274176}.
CC -!- INDUCTION: Up-regulated by bacterial lipopolysaccharide (LPS) (at
CC protein level) (PubMed:15793005). By bacterial lipopolysaccharide (LPS)
CC and by p53/TP53 (PubMed:9305847, PubMed:10200294). In monocytes by the
CC Bacillus Calmette-Guerin (BCG) (PubMed:11274176).
CC {ECO:0000269|PubMed:10200294, ECO:0000269|PubMed:11274176,
CC ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:9305847}.
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX and NEDD4.
CC {ECO:0000269|PubMed:15064722, ECO:0000269|PubMed:27927196}.
CC -!- DOMAIN: The LITAF domain is stabilized by a bound zinc ion
CC (PubMed:27927196, PubMed:27582497). The LITAF domain contains an
CC amphipathic helix that mediates interaction with lipid membranes
CC (PubMed:23166352, PubMed:27927196, PubMed:27582497). It interacts
CC specifically with phosphatidylethanolamine lipid headgroups, but not
CC with phosphoglycerol, phosphocholine, phosphoserine or
CC inositolhexakisphosphate (PubMed:27927196).
CC {ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:27582497,
CC ECO:0000269|PubMed:27927196}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to EGF.
CC {ECO:0000269|PubMed:23166352}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 1C (CMT1C) [MIM:601098]: A
CC dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder
CC of the peripheral nervous system, characterized by progressive weakness
CC and atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are
CC characterized by severely reduced nerve conduction velocities (less
CC than 38 m/sec), segmental demyelination and remyelination with onion
CC bulb formations on nerve biopsy, slowly progressive distal muscle
CC atrophy and weakness, absent deep tendon reflexes, and hollow feet.
CC {ECO:0000269|PubMed:12525712, ECO:0000269|PubMed:15776429,
CC ECO:0000269|PubMed:15786462, ECO:0000269|PubMed:16118794,
CC ECO:0000269|PubMed:21896645, ECO:0000269|PubMed:23166352,
CC ECO:0000269|PubMed:24604904}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in LITAF may be involved in extramammary Paget
CC disease (EMPD) carcinogenesis. EMPD is a cancerous disease representing
CC about 8% of all malignant skin cancers; it usually appears in the
CC anogenital area and can be fatal by metastasizing to internal organs
CC when left untreated for a long time. The clinical features are usually
CC those of eczematous eruptions with weeping and crust formation.
CC {ECO:0000269|PubMed:15197774}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a frameshift that creates an
CC unconventional splicing site. Data inferred from this isoform must be
CC interpreted with caution. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC URL="https://uantwerpen.vib.be/CMTMutations";
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DR EMBL; AF010312; AAC39530.1; -; mRNA.
DR EMBL; U77396; AAB36550.1; -; mRNA.
DR EMBL; AB034747; BAB32547.1; -; mRNA.
DR EMBL; AK095955; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX537543; CAD97778.1; -; mRNA.
DR EMBL; AC007616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85150.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85151.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85152.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85153.1; -; Genomic_DNA.
DR EMBL; BC000053; AAH00053.1; -; mRNA.
DR EMBL; BC008309; AAH08309.1; -; mRNA.
DR EMBL; BC016491; AAH16491.1; -; mRNA.
DR EMBL; BC039840; AAH39840.1; -; mRNA.
DR EMBL; BC046154; AAH46154.1; -; mRNA.
DR EMBL; BC096063; AAH96063.1; -; mRNA.
DR EMBL; BC096065; AAH96065.1; -; mRNA.
DR EMBL; BC096066; AAH96066.1; -; mRNA.
DR EMBL; BC101401; AAI01402.1; -; mRNA.
DR EMBL; BC101402; AAI01403.1; -; mRNA.
DR EMBL; BC101969; AAI01970.1; -; mRNA.
DR CCDS; CCDS32386.1; -. [Q99732-1]
DR CCDS; CCDS45411.1; -. [Q99732-3]
DR RefSeq; NP_001129944.1; NM_001136472.1. [Q99732-1]
DR RefSeq; NP_001129945.1; NM_001136473.1. [Q99732-3]
DR RefSeq; NP_004853.2; NM_004862.3. [Q99732-1]
DR RefSeq; XP_006721045.1; XM_006720982.2. [Q99732-1]
DR RefSeq; XP_006721046.1; XM_006720983.3. [Q99732-1]
DR RefSeq; XP_006721047.1; XM_006720984.3. [Q99732-1]
DR RefSeq; XP_006721048.1; XM_006720985.3. [Q99732-1]
DR RefSeq; XP_016879385.1; XM_017023896.1. [Q99732-1]
DR AlphaFoldDB; Q99732; -.
DR BioGRID; 114893; 79.
DR CORUM; Q99732; -.
DR IntAct; Q99732; 89.
DR STRING; 9606.ENSP00000459533; -.
DR BindingDB; Q99732; -.
DR iPTMnet; Q99732; -.
DR PhosphoSitePlus; Q99732; -.
DR SwissPalm; Q99732; -.
DR BioMuta; LITAF; -.
DR DMDM; 83304387; -.
DR jPOST; Q99732; -.
DR MassIVE; Q99732; -.
DR PaxDb; Q99732; -.
DR PeptideAtlas; Q99732; -.
DR PRIDE; Q99732; -.
DR ProteomicsDB; 33961; -.
DR ProteomicsDB; 78448; -. [Q99732-1]
DR ProteomicsDB; 78449; -. [Q99732-2]
DR Antibodypedia; 1839; 297 antibodies from 36 providers.
DR DNASU; 9516; -.
DR Ensembl; ENST00000339430.9; ENSP00000340118.5; ENSG00000189067.14. [Q99732-1]
DR Ensembl; ENST00000413364.6; ENSP00000397958.2; ENSG00000189067.14. [Q99732-3]
DR Ensembl; ENST00000570904.5; ENSP00000459138.1; ENSG00000189067.14. [Q99732-1]
DR Ensembl; ENST00000571688.5; ENSP00000459533.1; ENSG00000189067.14. [Q99732-1]
DR Ensembl; ENST00000574763.5; ENSP00000461813.1; ENSG00000189067.14. [Q99732-1]
DR Ensembl; ENST00000576036.5; ENSP00000461667.1; ENSG00000189067.14. [Q99732-1]
DR Ensembl; ENST00000622633.5; ENSP00000483114.1; ENSG00000189067.14. [Q99732-1]
DR GeneID; 9516; -.
DR KEGG; hsa:9516; -.
DR MANE-Select; ENST00000622633.5; ENSP00000483114.1; NM_001136472.2; NP_001129944.1.
DR UCSC; uc002daz.4; human. [Q99732-1]
DR CTD; 9516; -.
DR DisGeNET; 9516; -.
DR GeneCards; LITAF; -.
DR GeneReviews; LITAF; -.
DR HGNC; HGNC:16841; LITAF.
DR HPA; ENSG00000189067; Low tissue specificity.
DR MalaCards; LITAF; -.
DR MIM; 601098; phenotype.
DR MIM; 603795; gene.
DR neXtProt; NX_Q99732; -.
DR OpenTargets; ENSG00000189067; -.
DR Orphanet; 101083; Charcot-Marie-Tooth disease type 1C.
DR PharmGKB; PA134879224; -.
DR VEuPathDB; HostDB:ENSG00000189067; -.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR GeneTree; ENSGT00940000155366; -.
DR HOGENOM; CLU_095549_3_0_1; -.
DR InParanoid; Q99732; -.
DR OMA; SCMDVHH; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; Q99732; -.
DR TreeFam; TF313294; -.
DR PathwayCommons; Q99732; -.
DR SignaLink; Q99732; -.
DR SIGNOR; Q99732; -.
DR BioGRID-ORCS; 9516; 20 hits in 1094 CRISPR screens.
DR ChiTaRS; LITAF; human.
DR GeneWiki; LITAF; -.
DR GenomeRNAi; 9516; -.
DR Pharos; Q99732; Tbio.
DR PRO; PR:Q99732; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q99732; protein.
DR Bgee; ENSG00000189067; Expressed in blood and 206 other tissues.
DR ExpressionAtlas; Q99732; baseline and differential.
DR Genevisible; Q99732; HS.
DR GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IDA:UniProtKB.
DR GO; GO:0098560; C:cytoplasmic side of late endosome membrane; IDA:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0010935; P:regulation of macrophage cytokine production; IEA:Ensembl.
DR InterPro; IPR006629; LITAF.
DR InterPro; IPR037519; LITAF_fam.
DR PANTHER; PTHR23292; PTHR23292; 1.
DR Pfam; PF10601; zf-LITAF-like; 1.
DR SMART; SM00714; LITAF; 1.
DR PROSITE; PS51837; LITAF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Charcot-Marie-Tooth disease;
KW Cytoplasm; Disease variant; DNA-binding; Endosome; Golgi apparatus;
KW Lysosome; Membrane; Metal-binding; Neurodegeneration; Neuropathy; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..161
FT /note="Lipopolysaccharide-induced tumor necrosis factor-
FT alpha factor"
FT /id="PRO_0000084440"
FT DOMAIN 76..160
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..134
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000269|PubMed:27927196"
FT MOTIF 17..20
FT /note="PSAP motif; important for interaction with TSG101"
FT /evidence="ECO:0000269|PubMed:16118794,
FT ECO:0000269|PubMed:23166352"
FT MOTIF 20..23
FT /note="PPxY motif"
FT /evidence="ECO:0000269|PubMed:15064722,
FT ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:27927196"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:27582497,
FT ECO:0000305|PubMed:27927196"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:27927196"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:27582497,
FT ECO:0000305|PubMed:27927196"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:27927196"
FT VAR_SEQ 127..161
FT /note="CIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL -> VHSGLLLHPLLRG
FT CPAGRGPLLSQLQSSPGHLQAFVGLSQTWREPGAAGSPFHLSSSFTPGGGSALVVSPLQ
FT GAHLHVFFWGEYVAKLTNLQTPEIAAWSRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10200294,
FT ECO:0000303|PubMed:9305847"
FT /id="VSP_016461"
FT VAR_SEQ 127..161
FT /note="CIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL -> QECSGTIVALRSF
FT DLLGSCNPPSSAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045701"
FT VARIANT 23
FT /note="Y -> H (in one EMPD primary tumor; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:15197774"
FT /id="VAR_024014"
FT VARIANT 49
FT /note="T -> M (in CMT1C; dbSNP:rs141862602)"
FT /evidence="ECO:0000269|PubMed:15776429"
FT /id="VAR_024015"
FT VARIANT 92
FT /note="I -> V (in dbSNP:rs4280262)"
FT /evidence="ECO:0000269|PubMed:15776429,
FT ECO:0000269|PubMed:15786462"
FT /id="VAR_024016"
FT VARIANT 112
FT /note="G -> S (in CMT1C; does not abolish interaction with
FT NEDD4 and TSG101; dbSNP:rs104894519)"
FT /evidence="ECO:0000269|PubMed:12525712,
FT ECO:0000269|PubMed:15776429, ECO:0000269|PubMed:15786462,
FT ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:24604904"
FT /id="VAR_024017"
FT VARIANT 115
FT /note="T -> N (in CMT1C; does not abolish interaction with
FT NEDD4 and TSG101; dbSNP:rs104894520)"
FT /evidence="ECO:0000269|PubMed:12525712,
FT ECO:0000269|PubMed:16118794"
FT /id="VAR_024018"
FT VARIANT 116
FT /note="W -> G (in CMT1C; decreases protein stability and
FT association with early endosome membranes; impaired
FT function in targeting endocytosed proteins for lysosomal
FT degradation; does not abolish interaction with NEDD4 and
FT TSG101; dbSNP:rs104894521)"
FT /evidence="ECO:0000269|PubMed:12525712,
FT ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:21896645,
FT ECO:0000269|PubMed:23166352"
FT /id="VAR_024019"
FT VARIANT 122
FT /note="L -> V (in CMT1C; dbSNP:rs104894522)"
FT /evidence="ECO:0000269|PubMed:15776429"
FT /id="VAR_024020"
FT MUTAGEN 17..20
FT /note="PSAP->ASAA: Impaired function in targeting
FT endocytosed proteins for lysosomal degradation."
FT /evidence="ECO:0000269|PubMed:23166352"
FT MUTAGEN 17..19
FT /note="PSA->AGG: Abolishes interaction with TSG101."
FT /evidence="ECO:0000269|PubMed:16118794"
FT MUTAGEN 23
FT /note="Y->A: Abolishes interaction with NEDD4."
FT /evidence="ECO:0000269|PubMed:16118794"
FT MUTAGEN 23
FT /note="Y->A: Abolishes interaction with WWOX. Abolishes
FT interaction with NEDD4. Abolishes interaction with NEDD4
FT and impairs location at endosomes; when associated with A-
FT 61."
FT /evidence="ECO:0000269|PubMed:15064722,
FT ECO:0000269|PubMed:27927196"
FT MUTAGEN 61
FT /note="Y->A: No effect on interaction with WWOX. No effect
FT on interaction with NEDD4. Abolishes interaction with NEDD4
FT and impairs location at endosomes; when associated with A-
FT 23."
FT /evidence="ECO:0000269|PubMed:15064722,
FT ECO:0000269|PubMed:27927196"
FT MUTAGEN 96
FT /note="C->A: Abolishes association with cytoplasmic vesicle
FT membranes."
FT /evidence="ECO:0000269|PubMed:27582497"
FT MUTAGEN 135
FT /note="P->T: Decreases protein stability and association
FT with early endosome membranes. Impaired function in
FT targeting endocytosed proteins for lysosomal degradation."
FT /evidence="ECO:0000269|PubMed:21896645,
FT ECO:0000269|PubMed:23166352"
FT MUTAGEN 144
FT /note="V->M: No effect on location at endosomes, but
FT impairs protein stability."
FT /evidence="ECO:0000269|PubMed:27927196"
FT MUTAGEN 148
FT /note="C->A: Abolishes association with cytoplasmic vesicle
FT membranes."
FT /evidence="ECO:0000269|PubMed:27582497"
FT VARIANT Q99732-2:174
FT /note="A -> S (found as a somatic mutation in a EMPD
FT primary tumor)"
FT /evidence="ECO:0000305"
FT /id="VAR_082859"
SQ SEQUENCE 161 AA; 17107 MW; 08D15BF1FDCA16F0 CRC64;
MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS
YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG
SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L
