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Lipopolysaccharide-induced tumor necrosis factor-alpha factor (LPS-induced TNF-alpha factor) (Small integral membrane protein of lysosome/late endosome) (p53-induced gene 7 protein)

 LITAF_HUMAN             Reviewed;         161 AA.
Q99732; D3DUG1; G5E9K0; Q05DW0; Q9C0L6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
22-NOV-2017, entry version 159.
RecName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha factor {ECO:0000303|PubMed:10200294};
Short=LPS-induced TNF-alpha factor {ECO:0000303|PubMed:10200294};
AltName: Full=Small integral membrane protein of lysosome/late endosome {ECO:0000303|PubMed:11274176};
AltName: Full=p53-induced gene 7 protein {ECO:0000303|PubMed:11274176};
Name=LITAF;
Synonyms=PIG7 {ECO:0000303|PubMed:11274176,
ECO:0000303|PubMed:15197774}, SIMPLE {ECO:0000303|PubMed:11274176};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION BY TP53.
TISSUE=Colon cancer;
PubMed=9305847; DOI=10.1038/38525;
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
"A model for p53-induced apoptosis.";
Nature 389:300-306(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, AND
TISSUE SPECIFICITY.
TISSUE=Monocyte;
PubMed=10200294; DOI=10.1073/pnas.96.8.4518;
Myokai F., Takashiba S., Lebo R., Amar S.;
"A novel lipopolysaccharide-induced transcription factor regulating
tumor necrosis factor alpha gene expression: molecular cloning,
sequencing, characterization, and chromosomal assignment.";
Proc. Natl. Acad. Sci. U.S.A. 96:4518-4523(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION,
AND SUBCELLULAR LOCATION.
TISSUE=Monocyte;
PubMed=11274176; DOI=10.1074/jbc.M011660200;
Moriwaki Y., Begum N.A., Kobayashi M., Matsumoto M., Toyoshima K.,
Seya T.;
"Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall
complex induce a novel lysosomal membrane protein, SIMPLE, that
bridges the missing link between lipopolysaccharide and p53-inducible
gene, LITAF(PIG7), and estrogen-inducible gene, EET-1.";
J. Biol. Chem. 276:23065-23076(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Hair follicle dermal papilla;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Esophageal carcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney, Pancreas, PNS, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH WWOX, DOMAIN, AND MUTAGENESIS OF TYR-23 AND TYR-61.
PubMed=15064722; DOI=10.1038/sj.onc.1207680;
Ludes-Meyers J.H., Kil H., Bednarek A.K., Drake J., Bedford M.T.,
Aldaz C.M.;
"WWOX binds the specific proline-rich ligand PPXY: identification of
candidate interacting proteins.";
Oncogene 23:5049-5055(2004).
[10]
INTERACTION WITH NEDD4 AND TSG101, CHARACTERIZATION OF VARIANTS CMT1C
SER-112; ASN-115 AND GLY-116, AND MUTAGENESIS OF 17-PRO--ALA-19 AND
TYR-23.
PubMed=16118794; DOI=10.1002/jnr.20628;
Shirk A.J., Anderson S.K., Hashemi S.H., Chance P.F., Bennett C.L.;
"SIMPLE interacts with NEDD4 and TSG101: evidence for a role in
lysosomal sorting and implications for Charcot-Marie-Tooth disease.";
J. Neurosci. Res. 82:43-50(2005).
[11]
FUNCTION, INTERACTION WITH STAT6, SUBCELLULAR LOCATION, AND INDUCTION
BY LIPOPOLYSACCHARIDE.
PubMed=15793005; DOI=10.1073/pnas.0501159102;
Tang X., Marciano D.L., Leeman S.E., Amar S.;
"LPS induces the interaction of a transcription factor, LPS-induced
TNF-alpha factor, and STAT6(B) with effects on multiple cytokines.";
Proc. Natl. Acad. Sci. U.S.A. 102:5132-5137(2005).
[12]
SUBCELLULAR LOCATION.
PubMed=16954198; DOI=10.1073/pnas.0605988103;
Tang X., Metzger D., Leeman S., Amar S.;
"LPS-induced TNF-alpha factor (LITAF)-deficient mice express reduced
LPS-induced cytokine: Evidence for LITAF-dependent LPS signaling
pathways.";
Proc. Natl. Acad. Sci. U.S.A. 103:13777-13782(2006).
[13]
SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-135, AND CHARACTERIZATION OF
VARIANT CMT1C GLY-116.
PubMed=21896645; DOI=10.1242/jcs.087114;
Lee S.M., Olzmann J.A., Chin L.S., Li L.;
"Mutations associated with Charcot-Marie-Tooth disease cause SIMPLE
protein mislocalization and degradation by the proteasome and
aggresome-autophagy pathways.";
J. Cell Sci. 124:3319-3331(2011).
[14]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH TSG101; STAM
AND HGS, PHOSPHORYLATION, MUTAGENESIS OF 17-PRO--PRO-20 AND PRO-135,
AND CHARACTERIZATION OF VARIANT CMT1C GLY-116.
PubMed=23166352; DOI=10.1083/jcb.201204137;
Lee S.M., Chin L.S., Li L.;
"Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the
ESCRT machinery in endosomal trafficking.";
J. Cell Biol. 199:799-816(2012).
[15]
3D-STRUCTURE MODELING, NMR SECONDARY STRUCTURE ANALYSIS, SUBCELLULAR
LOCATION, TOPOLOGY, ZINC-BINDING, SUBUNIT, INTERACTION WITH NEDD4,
DOMAIN, AND MUTAGENESIS OF TYR-23; TYR-61 AND VAL-144.
PubMed=27927196; DOI=10.1186/s12915-016-0332-8;
Ho A.K., Wagstaff J.L., Manna P.T., Wartosch L., Qamar S.,
Garman E.F., Freund S.M., Roberts R.C.;
"The topology, structure and PE interaction of LITAF underpin a
Charcot-Marie-Tooth disease type 1C.";
BMC Biol. 14:109-109(2016).
[16]
ZINC-BINDING, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYS-96
AND CYS-148, AND DOMAIN.
PubMed=27582497; DOI=10.1042/BCJ20160657;
Qin W., Wunderley L., Barrett A.L., High S., Woodman P.G.;
"The Charcot Marie Tooth disease protein LITAF is a zinc-binding
monotopic membrane protein.";
Biochem. J. 473:3965-3978(2016).
[17]
VARIANTS CMT1C SER-112; ASN-115 AND GLY-116.
PubMed=12525712; DOI=10.1212/WNL.60.1.22;
Street V.A., Bennett C.L., Goldy J.D., Shirk A.J., Kleopa K.A.,
Tempel B.L., Lipe H.P., Scherer S.S., Bird T.D., Chance P.F.;
"Mutation of a putative protein degradation gene LITAF/SIMPLE in
Charcot-Marie-Tooth disease 1C.";
Neurology 60:22-26(2003).
[18]
VARIANT EMPD HIS-23.
PubMed=15197774; DOI=10.1002/ijc.20251;
Matsumura Y., Matsumura Y., Nishigori C., Horio T., Miyachi Y.;
"PIG7/LITAF gene mutation and overexpression of its gene product in
extramammary Paget's disease.";
Int. J. Cancer 111:218-223(2004).
[19]
VARIANT CMT1C SER-112, AND VARIANT VAL-92.
PubMed=15786462; DOI=10.1002/ana.20434;
Meggouh F., de Visser M., Arts W.F.M., De Coo R.I.F.M.,
van Schaik I.N., Baas F.;
"Early onset neuropathy in a compound form of Charcot-Marie-Tooth
disease.";
Ann. Neurol. 57:589-591(2005).
[20]
VARIANTS CMT1C MET-49; SER-112 AND VAL-122, VARIANT VAL-92, AND
PUTATIVE FUNCTION.
PubMed=15776429; DOI=10.1002/humu.20153;
Saifi G.M., Szigeti K., Wiszniewski W., Shy M.E., Krajewski K.,
Hausmanowa-Petrusewicz I., Kochanski A., Reeser S., Mancias P.,
Butler I., Lupski J.R.;
"SIMPLE mutations in Charcot-Marie-Tooth disease and the potential
role of its protein product in protein degradation.";
Hum. Mutat. 25:372-383(2005).
-!- FUNCTION: Plays a role in endosomal protein trafficking and in
targeting proteins for lysosomal degradation (PubMed:23166352).
Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal
degradation, and thereby helps downregulate downstream signaling
cascades (PubMed:23166352). Helps recruit the ESCRT complex
components TSG101, HGS and STAM to cytoplasmic membranes
(PubMed:23166352). Probably plays a role in regulating protein
degradation via its interaction with NEDD4 (PubMed:15776429). May
also contribute to the regulation of gene expression in the
nucleus (PubMed:10200294, PubMed:15793005). Binds DNA (in vitro)
and may play a synergistic role with STAT6 in the nucleus in
regulating the expression of various cytokines (PubMed:15793005).
May regulate the expression of numerous cytokines, such as TNF,
CCL2, CCL5, CXCL1, IL1A and IL10 (PubMed:10200294,
PubMed:15793005). {ECO:0000269|PubMed:15793005,
ECO:0000269|PubMed:23166352, ECO:0000303|PubMed:15776429,
ECO:0000305|PubMed:10200294}.
-!- SUBUNIT: Monomer (PubMed:27927196). Interacts with NEDD4
(PubMed:16118794, PubMed:27927196). Interacts (via PSAP motif)
with TSG101, a component of the ESCRT-I complex (endosomal sorting
complex required for transport I) (PubMed:16118794). Interacts
with WWOX (PubMed:15064722). Interacts with STAM, a component of
the ESCRT-0 complex; the interaction is direct (PubMed:23166352).
Identified in a complex with STAM and HGS; within this complex,
interacts directly with STAM, but not with HGS (PubMed:23166352).
Interacts with STAT6 (PubMed:15793005).
{ECO:0000269|PubMed:15064722, ECO:0000269|PubMed:16118794,
ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:27927196,
ECO:0000305|PubMed:15793005}.
-!- INTERACTION:
O95817:BAG3; NbExp=7; IntAct=EBI-725647, EBI-747185;
Q13137:CALCOCO2; NbExp=7; IntAct=EBI-725647, EBI-739580;
I6L9I8:EPN3; NbExp=4; IntAct=EBI-725647, EBI-12866582;
O14964:HGS; NbExp=7; IntAct=EBI-725647, EBI-740220;
P46934:NEDD4; NbExp=4; IntAct=EBI-725647, EBI-726944;
Q96CV9-2:OPTN; NbExp=3; IntAct=EBI-725647, EBI-9091423;
Q96HR9:REEP6; NbExp=7; IntAct=EBI-725647, EBI-750345;
O75886:STAM2; NbExp=9; IntAct=EBI-725647, EBI-373258;
Q99816:TSG101; NbExp=3; IntAct=EBI-725647, EBI-346882;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-725647, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=7; IntAct=EBI-725647, EBI-10173939;
Q9NZC7:WWOX; NbExp=5; IntAct=EBI-725647, EBI-4320739;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15793005}.
Nucleus {ECO:0000269|PubMed:15793005,
ECO:0000269|PubMed:16954198}. Lysosome membrane
{ECO:0000269|PubMed:11274176, ECO:0000269|PubMed:27582497};
Peripheral membrane protein {ECO:0000269|PubMed:11274176};
Cytoplasmic side {ECO:0000269|PubMed:11274176}. Early endosome
membrane {ECO:0000269|PubMed:21896645,
ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:27582497}. Late
endosome membrane {ECO:0000269|PubMed:27582497}. Endosome membrane
{ECO:0000269|PubMed:27927196}; Peripheral membrane protein
{ECO:0000269|PubMed:27927196}; Cytoplasmic side
{ECO:0000269|PubMed:27927196}. Cell membrane
{ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:27582497};
Peripheral membrane protein {ECO:0000269|PubMed:27582497};
Cytoplasmic side {ECO:0000269|PubMed:27582497}. Golgi apparatus
membrane {ECO:0000269|PubMed:16118794}. Note=Associated with
membranes of lysosomes, early and late endosomes (PubMed:11274176,
PubMed:27927196, PubMed:27582497). Can translocate from the
cytoplasm into the nucleus (PubMed:15793005). Detected at Schmidt-
Lanterman incisures and in nodal regions of myelinating Schwann
cells (By similarity). {ECO:0000250|UniProtKB:Q9JLJ0,
ECO:0000269|PubMed:11274176, ECO:0000269|PubMed:15793005,
ECO:0000269|PubMed:27582497, ECO:0000269|PubMed:27927196}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99732-1; Sequence=Displayed;
Name=2;
IsoId=Q99732-2; Sequence=VSP_016461;
Note=May be due to a frameshift that creates an unconventional
splicing site. Data inferred from this isoform must be
interpreted with caution. Variant in position: 174:A->S (found
as a somatic mutation in a EMPD primary tumor).;
Name=3;
IsoId=Q99732-3; Sequence=VSP_045701;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously and abundantly expressed.
Expressed predominantly in the placenta, peripheral blood
leukocytes, lymph nodes and spleen. {ECO:0000269|PubMed:10200294,
ECO:0000269|PubMed:11274176}.
-!- INDUCTION: Up-regulated by bacterial lipopolysaccharide (LPS) (at
protein level) (PubMed:15793005). By bacterial lipopolysaccharide
(LPS) and by p53/TP53 (PubMed:9305847, PubMed:10200294). In
monocytes by the Bacillus Calmette-Guerin (BCG) (PubMed:11274176).
{ECO:0000269|PubMed:10200294, ECO:0000269|PubMed:11274176,
ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:9305847}.
-!- DOMAIN: The PPxY motif mediates interaction with WWOX and NEDD4.
{ECO:0000269|PubMed:15064722, ECO:0000269|PubMed:27927196}.
-!- DOMAIN: The LITAF domain is stabilized by a bound zinc ion
(PubMed:27927196, PubMed:27582497). The LITAF domain contains an
amphiphatic helix that mediates interaction with lipid membranes
(PubMed:23166352, PubMed:27927196, PubMed:27582497). It interacts
specifically with phosphatidylethanolamine lipid headgroups, but
not with phosphoglycerol, phosphocholine, phosphoserine or
inositolhexakisphosphate (PubMed:27927196).
{ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:27582497,
ECO:0000269|PubMed:27927196}.
-!- PTM: Phosphorylated on tyrosine residues in response to EGF.
{ECO:0000269|PubMed:23166352}.
-!- DISEASE: Charcot-Marie-Tooth disease 1C (CMT1C) [MIM:601098]: A
dominant demyelinating form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. Charcot-
Marie-Tooth disease is classified in two main groups on the basis
of electrophysiologic properties and histopathology: primary
peripheral demyelinating neuropathies (designated CMT1 when they
are dominantly inherited) and primary peripheral axonal
neuropathies (CMT2). Demyelinating neuropathies are characterized
by severely reduced nerve conduction velocities (less than 38
m/sec), segmental demyelination and remyelination with onion bulb
formations on nerve biopsy, slowly progressive distal muscle
atrophy and weakness, absent deep tendon reflexes, and hollow
feet. {ECO:0000269|PubMed:12525712, ECO:0000269|PubMed:15776429,
ECO:0000269|PubMed:15786462, ECO:0000269|PubMed:16118794,
ECO:0000269|PubMed:21896645, ECO:0000269|PubMed:23166352}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Defects in LITAF may be involved in extramammary
Paget disease (EMPD) carcinogenesis. EMPD is a cancerous disease
representing about 8% of all malignant skin cancers; it usually
appears in the anogenital area and can be fatal by metastasizing
to internal organs when left untreated for a long time. The
clinical features are usually those of eczematous eruptions with
weeping and crust formation. {ECO:0000269|PubMed:15197774}.
-!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="http://www.molgen.ua.ac.be/CMTMutations/";
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EMBL; AF010312; AAC39530.1; -; mRNA.
EMBL; U77396; AAB36550.1; -; mRNA.
EMBL; AB034747; BAB32547.1; -; mRNA.
EMBL; AK095955; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BX537543; CAD97778.1; -; mRNA.
EMBL; AC007616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85150.1; -; Genomic_DNA.
EMBL; CH471112; EAW85151.1; -; Genomic_DNA.
EMBL; CH471112; EAW85152.1; -; Genomic_DNA.
EMBL; CH471112; EAW85153.1; -; Genomic_DNA.
EMBL; BC000053; AAH00053.1; -; mRNA.
EMBL; BC008309; AAH08309.1; -; mRNA.
EMBL; BC016491; AAH16491.1; -; mRNA.
EMBL; BC039840; AAH39840.1; -; mRNA.
EMBL; BC046154; AAH46154.1; -; mRNA.
EMBL; BC096063; AAH96063.1; -; mRNA.
EMBL; BC096065; AAH96065.1; -; mRNA.
EMBL; BC096066; AAH96066.1; -; mRNA.
EMBL; BC101401; AAI01402.1; -; mRNA.
EMBL; BC101402; AAI01403.1; -; mRNA.
EMBL; BC101969; AAI01970.1; -; mRNA.
CCDS; CCDS32386.1; -. [Q99732-1]
CCDS; CCDS45411.1; -. [Q99732-3]
RefSeq; NP_001129944.1; NM_001136472.1. [Q99732-1]
RefSeq; NP_001129945.1; NM_001136473.1. [Q99732-3]
RefSeq; NP_004853.2; NM_004862.3. [Q99732-1]
RefSeq; XP_006721045.1; XM_006720982.2. [Q99732-1]
RefSeq; XP_006721046.1; XM_006720983.3. [Q99732-1]
RefSeq; XP_006721047.1; XM_006720984.3. [Q99732-1]
RefSeq; XP_006721048.1; XM_006720985.3. [Q99732-1]
RefSeq; XP_016879385.1; XM_017023896.1. [Q99732-1]
UniGene; Hs.459940; -.
ProteinModelPortal; Q99732; -.
BioGrid; 114893; 40.
IntAct; Q99732; 34.
MINT; MINT-1391850; -.
STRING; 9606.ENSP00000340118; -.
iPTMnet; Q99732; -.
PhosphoSitePlus; Q99732; -.
BioMuta; LITAF; -.
DMDM; 83304387; -.
EPD; Q99732; -.
PaxDb; Q99732; -.
PeptideAtlas; Q99732; -.
PRIDE; Q99732; -.
DNASU; 9516; -.
Ensembl; ENST00000339430; ENSP00000340118; ENSG00000189067. [Q99732-1]
Ensembl; ENST00000381810; ENSP00000371231; ENSG00000189067. [Q99732-2]
Ensembl; ENST00000413364; ENSP00000397958; ENSG00000189067. [Q99732-3]
Ensembl; ENST00000570904; ENSP00000459138; ENSG00000189067. [Q99732-1]
Ensembl; ENST00000571688; ENSP00000459533; ENSG00000189067. [Q99732-1]
Ensembl; ENST00000574763; ENSP00000461813; ENSG00000189067. [Q99732-1]
Ensembl; ENST00000576036; ENSP00000461667; ENSG00000189067. [Q99732-1]
Ensembl; ENST00000620789; ENSP00000481589; ENSG00000189067. [Q99732-3]
Ensembl; ENST00000622633; ENSP00000483114; ENSG00000189067. [Q99732-1]
GeneID; 9516; -.
KEGG; hsa:9516; -.
UCSC; uc002daz.4; human. [Q99732-1]
CTD; 9516; -.
DisGeNET; 9516; -.
EuPathDB; HostDB:ENSG00000189067.12; -.
GeneCards; LITAF; -.
GeneReviews; LITAF; -.
H-InvDB; HIX0134387; -.
HGNC; HGNC:16841; LITAF.
HPA; HPA006960; -.
MalaCards; LITAF; -.
MIM; 601098; phenotype.
MIM; 603795; gene.
neXtProt; NX_Q99732; -.
OpenTargets; ENSG00000189067; -.
Orphanet; 101083; Charcot-Marie-Tooth disease type 1C.
PharmGKB; PA134879224; -.
eggNOG; ENOG410IVVU; Eukaryota.
eggNOG; ENOG41122PJ; LUCA.
GeneTree; ENSGT00540000071542; -.
HOGENOM; HOG000039585; -.
HOVERGEN; HBG006272; -.
InParanoid; Q99732; -.
KO; K19363; -.
OMA; VYVQPGL; -.
OrthoDB; EOG091G0XNM; -.
PhylomeDB; Q99732; -.
TreeFam; TF313294; -.
SIGNOR; Q99732; -.
ChiTaRS; LITAF; human.
GeneWiki; LITAF; -.
GenomeRNAi; 9516; -.
PRO; PR:Q99732; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000189067; -.
CleanEx; HS_LITAF; -.
ExpressionAtlas; Q99732; baseline and differential.
Genevisible; Q99732; HS.
GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IDA:UniProtKB.
GO; GO:0098560; C:cytoplasmic side of late endosome membrane; IDA:UniProtKB.
GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IC:NTNU_SB.
GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:NTNU_SB.
GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
InterPro; IPR006629; LITAF.
Pfam; PF10601; zf-LITAF-like; 1.
SMART; SM00714; LITAF; 1.
PROSITE; PS51837; LITAF; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Charcot-Marie-Tooth disease;
Complete proteome; Cytoplasm; Disease mutation; DNA-binding; Endosome;
Golgi apparatus; Lysosome; Membrane; Metal-binding; Neurodegeneration;
Neuropathy; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Zinc.
CHAIN 1 161 Lipopolysaccharide-induced tumor necrosis
factor-alpha factor.
/FTId=PRO_0000084440.
DOMAIN 76 160 LITAF. {ECO:0000255|PROSITE-
ProRule:PRU01181}.
REGION 111 134 Membrane-binding amphipathic helix.
{ECO:0000269|PubMed:27927196}.
MOTIF 17 20 PSAP motif; important for interaction
with TSG101.
{ECO:0000269|PubMed:16118794,
ECO:0000269|PubMed:23166352}.
MOTIF 20 23 PPxY motif. {ECO:0000269|PubMed:15064722,
ECO:0000269|PubMed:23166352,
ECO:0000269|PubMed:27927196}.
METAL 96 96 Zinc. {ECO:0000305|PubMed:27582497,
ECO:0000305|PubMed:27927196}.
METAL 99 99 Zinc. {ECO:0000305|PubMed:27927196}.
METAL 148 148 Zinc. {ECO:0000305|PubMed:27582497,
ECO:0000305|PubMed:27927196}.
METAL 151 151 Zinc. {ECO:0000305|PubMed:27927196}.
VAR_SEQ 127 161 CIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL -> VH
SGLLLHPLLRGCPAGRGPLLSQLQSSPGHLQAFVGLSQTWR
EPGAAGSPFHLSSSFTPGGGSALVVSPLQGAHLHVFFWGEY
VAKLTNLQTPEIAAWSRA (in isoform 2).
{ECO:0000303|PubMed:10200294,
ECO:0000303|PubMed:9305847}.
/FTId=VSP_016461.
VAR_SEQ 127 161 CIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL -> QE
CSGTIVALRSFDLLGSCNPPSSAS (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045701.
VARIANT 23 23 Y -> H (in one EMPD primary tumor;
somatic mutation).
{ECO:0000269|PubMed:15197774}.
/FTId=VAR_024014.
VARIANT 49 49 T -> M (in CMT1C; dbSNP:rs141862602).
{ECO:0000269|PubMed:15776429}.
/FTId=VAR_024015.
VARIANT 92 92 I -> V (in dbSNP:rs4280262).
{ECO:0000269|PubMed:15776429,
ECO:0000269|PubMed:15786462}.
/FTId=VAR_024016.
VARIANT 112 112 G -> S (in CMT1C; does not abolish
interaction with NEDD4 and TSG101;
dbSNP:rs104894519).
{ECO:0000269|PubMed:12525712,
ECO:0000269|PubMed:15776429,
ECO:0000269|PubMed:15786462,
ECO:0000269|PubMed:16118794}.
/FTId=VAR_024017.
VARIANT 115 115 T -> N (in CMT1C; does not abolish
interaction with NEDD4 and TSG101;
dbSNP:rs104894520).
{ECO:0000269|PubMed:12525712,
ECO:0000269|PubMed:16118794}.
/FTId=VAR_024018.
VARIANT 116 116 W -> G (in CMT1C; decreases protein
stability and association with early
endosome membranes; impaired function in
targeting endocytosed proteins for
lysosomal degradation; does not abolish
interaction with NEDD4 and TSG101;
dbSNP:rs104894521).
{ECO:0000269|PubMed:12525712,
ECO:0000269|PubMed:16118794,
ECO:0000269|PubMed:21896645,
ECO:0000269|PubMed:23166352}.
/FTId=VAR_024019.
VARIANT 122 122 L -> V (in CMT1C; dbSNP:rs104894522).
{ECO:0000269|PubMed:15776429}.
/FTId=VAR_024020.
MUTAGEN 17 20 PSAP->ASAA: Impaired function in
targeting endocytosed proteins for
lysosomal degradation.
{ECO:0000269|PubMed:23166352}.
MUTAGEN 17 19 PSA->AGG: Abolishes interaction with
TSG101. {ECO:0000269|PubMed:16118794}.
MUTAGEN 23 23 Y->A: Abolishes interaction with NEDD4.
{ECO:0000269|PubMed:16118794}.
MUTAGEN 23 23 Y->A: Abolishes interaction with WWOX.
Abolishes interaction with NEDD4.
Abolishes interaction with NEDD4 and
impairs location at endosomes; when
associated with A-61.
{ECO:0000269|PubMed:15064722,
ECO:0000269|PubMed:27927196}.
MUTAGEN 61 61 Y->A: No effect on interaction with WWOX.
No effect on interaction with NEDD4.
Abolishes interaction with NEDD4 and
impairs location at endosomes; when
associated with A-23.
{ECO:0000269|PubMed:15064722,
ECO:0000269|PubMed:27927196}.
MUTAGEN 96 96 C->A: Abolishes association with
cytoplasmic vesicle membranes.
{ECO:0000269|PubMed:27582497}.
MUTAGEN 135 135 P->T: Decreases protein stability and
association with early endosome
membranes. Impaired function in targeting
endocytosed proteins for lysosomal
degradation.
{ECO:0000269|PubMed:21896645,
ECO:0000269|PubMed:23166352}.
MUTAGEN 144 144 V->M: No effect on location at endosomes,
but impairs protein stability.
{ECO:0000269|PubMed:27927196}.
MUTAGEN 148 148 C->A: Abolishes association with
cytoplasmic vesicle membranes.
{ECO:0000269|PubMed:27582497}.
SEQUENCE 161 AA; 17107 MW; 08D15BF1FDCA16F0 CRC64;
MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS
YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG
SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L


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