LIS1_HUMAN
ID LIS1_HUMAN Reviewed; 410 AA.
AC P43034; B2R7Q7; Q8WZ88; Q8WZ89;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit beta {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000305};
DE AltName: Full=Lissencephaly-1 protein {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=PAF acetylhydrolase 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=PAF-AH 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=PAF-AH alpha {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=PAFAH alpha {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAFAH1B1 {ECO:0000255|HAMAP-Rule:MF_03141,
GN ECO:0000312|HGNC:HGNC:8574};
GN Synonyms=LIS1 {ECO:0000255|HAMAP-Rule:MF_03141}, MDCR, MDS, PAFAHA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
RX PubMed=8355785; DOI=10.1038/364717a0;
RA Reiner O., Carrozzo R., Shen Y., Wehnert M., Faustinella F., Dobyns W.B.,
RA Caskey C.T., Ledbetter D.H.;
RT "Isolation of a Miller-Dieker lissencephaly gene containing G protein beta-
RT subunit-like repeats.";
RL Nature 364:717-721(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LIS1 ARG-149.
RX PubMed=9063735; DOI=10.1093/hmg/6.2.157;
RA Lo Nigro C., Chong S.S., Smith A.C.M., Dobyns W.B., Carrozzo R.,
RA Ledbetter D.H.;
RT "Point mutations and an intragenic deletion in LIS1, the lissencephaly
RT causative gene in isolated lissencephaly sequence and Miller-Dieker
RT syndrome.";
RL Hum. Mol. Genet. 6:157-164(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Zhao M.J., Xia S.L., Li T.P.;
RT "High expression of the lissencephaly gene in hepatocarcinoma patients.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Feng Z., Zhang B., Peng X., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 [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=Uterus;
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 DCX.
RX PubMed=11001923; DOI=10.1093/oxfordjournals.hmg.a018911;
RA Caspi M., Atlas R., Kantor A., Sapir T., Reiner O.;
RT "Interaction between LIS1 and doublecortin, two lissencephaly gene
RT products.";
RL Hum. Mol. Genet. 9:2205-2213(2000).
RN [10]
RP INTERACTION WITH NDE1, AND CHARACTERIZATION OF VARIANTS LIS1 ARG-149 AND
RP SBH PRO-169.
RX PubMed=11163258; DOI=10.1016/s0896-6273(00)00145-8;
RA Feng Y., Olson E.C., Stukenberg P.T., Flanagan L.A., Kirschner M.W.,
RA Walsh C.A.;
RT "LIS1 regulates CNS lamination by interacting with mNudE, a central
RT component of the centrosome.";
RL Neuron 28:665-679(2000).
RN [11]
RP SELF-ASSOCIATION, INTERACTION WITH RSN; DYNEIN AND DYNACTIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11889140; DOI=10.1083/jcb.200109046;
RA Tai C.-Y., Dujardin D.L., Faulkner N.E., Vallee R.B.;
RT "Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore
RT function.";
RL J. Cell Biol. 156:959-968(2002).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=11940666; DOI=10.1128/mcb.22.9.3089-3102.2002;
RA Coquelle F.M., Caspi M., Cordelieres F.P., Dompierre J.P., Dujardin D.L.,
RA Koifman C., Martin P., Hoogenraad C.C., Akhmanova A., Galjart N.,
RA De Mey J.R., Reiner O.;
RT "LIS1, CLIP-170's key to the dynein/dynactin pathway.";
RL Mol. Cell. Biol. 22:3089-3102(2002).
RN [13]
RP INTERACTION WITH NDEL1.
RX PubMed=12556484; DOI=10.1128/mcb.23.4.1239-1250.2003;
RA Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X.;
RT "Human Nudel and NudE as regulators of cytoplasmic dynein in poleward
RT protein transport along the mitotic spindle.";
RL Mol. Cell. Biol. 23:1239-1250(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [15]
RP INTERACTION WITH NDEL1.
RX PubMed=14970193; DOI=10.1083/jcb.200308058;
RA Liang Y., Yu W., Li Y., Yang Z., Yan X., Huang Q., Zhu X.;
RT "Nudel functions in membrane traffic mainly through association with Lis1
RT and cytoplasmic dynein.";
RL J. Cell Biol. 164:557-566(2004).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS LIS1
RP ARG-149; SBH PRO-169 AND LIS1 HIS-317.
RX PubMed=15173193; DOI=10.1083/jcb.200309025;
RA Tanaka T., Serneo F.F., Higgins C., Gambello M.J., Wynshaw-Boris A.,
RA Gleeson J.G.;
RT "Lis1 and doublecortin function with dynein to mediate coupling of the
RT nucleus to the centrosome in neuronal migration.";
RL J. Cell Biol. 165:709-721(2004).
RN [17]
RP INTERACTION WITH DISC1.
RX PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
RA Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
RA Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
RA Whiting P.J.;
RT "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
RT regulated protein complex: implications for schizophrenia and other major
RT neurological disorders.";
RL Mol. Cell. Neurosci. 25:42-55(2004).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH DCDC1.
RX PubMed=22159412; DOI=10.1242/jcs.085407;
RA Kaplan A., Reiner O.;
RT "Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody
RT during cytokinesis by the doublecortin domain-containing 5 protein.";
RL J. Cell Sci. 124:3989-4000(2011).
RN [21]
RP FUNCTION.
RX PubMed=22956769; DOI=10.1091/mbc.e12-03-0210;
RA Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I.,
RA Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C.,
RA King S.J., Akhmanova A.;
RT "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to
RT cellular structures.";
RL Mol. Biol. Cell 23:4226-4241(2012).
RN [22]
RP INTERACTION WITH INTS13.
RX PubMed=23097494; DOI=10.1091/mbc.e12-07-0558;
RA Jodoin J.N., Shboul M., Sitaram P., Zein-Sabatto H., Reversade B., Lee E.,
RA Lee L.A.;
RT "Human Asunder promotes dynein recruitment and centrosomal tethering to the
RT nucleus at mitotic entry.";
RL Mol. Biol. Cell 23:4713-4724(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP 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 [24]
RP VARIANT SBH PRO-169.
RX PubMed=10441340; DOI=10.1093/hmg/8.9.1757;
RA Pilz D.T., Kuc J., Matsumoto N., Bodurtha J., Bernadi B., Tassinari C.A.,
RA Dobyns W.B., Ledbetter D.H.;
RT "Subcortical band heterotopia in rare affected males can be caused by
RT missense mutations in DCX (XLIS) or LIS1.";
RL Hum. Mol. Genet. 8:1757-1760(1999).
RN [25]
RP VARIANTS LIS1 SER-31; SER-162 AND HIS-317.
RX PubMed=11502906; DOI=10.1212/wnl.57.3.416;
RA Leventer R.J., Cardoso C., Ledbetter D.H., Dobyns W.B.;
RT "LIS1 missense mutations cause milder lissencephaly phenotypes including a
RT child with normal IQ.";
RL Neurology 57:416-422(2001).
RN [26]
RP VARIANT SBH PRO-241.
RX PubMed=14581661; DOI=10.1212/wnl.61.8.1042;
RA Sicca F., Kelemen A., Genton P., Das S., Mei D., Moro F., Dobyns W.B.,
RA Guerrini R.;
RT "Mosaic mutations of the LIS1 gene cause subcortical band heterotopia.";
RL Neurology 61:1042-1046(2003).
RN [27]
RP VARIANT LIS1 PRO-277.
RX PubMed=15007136; DOI=10.1212/01.wnl.0000113725.46254.fd;
RA Torres F.R., Montenegro M.A., Marques-de-Faria A.P., Guerreiro M.M.,
RA Cendes F., Lopes-Cendes I.;
RT "Mutation screening in a cohort of patients with lissencephaly and
RT subcortical band heterotopia.";
RL Neurology 62:799-802(2004).
CC -!- FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I
CC platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an
CC enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2
CC position of PAF and its analogs and participates in PAF inactivation.
CC Regulates the PAF-AH (I) activity in a catalytic dimer composition-
CC dependent manner (By similarity). Required for proper activation of Rho
CC GTPases and actin polymerization at the leading edge of locomoting
CC cerebellar neurons and postmigratory hippocampal neurons in response to
CC calcium influx triggered via NMDA receptors (By similarity). Positively
CC regulates the activity of the minus-end directed microtubule motor
CC protein dynein. May enhance dynein-mediated microtubule sliding by
CC targeting dynein to the microtubule plus end. Required for several
CC dynein- and microtubule-dependent processes such as the maintenance of
CC Golgi integrity, the peripheral transport of microtubule fragments and
CC the coupling of the nucleus and centrosome. Required during brain
CC development for the proliferation of neuronal precursors and the
CC migration of newly formed neurons from the ventricular/subventricular
CC zone toward the cortical plate. Neuronal migration involves a process
CC called nucleokinesis, whereby migrating cells extend an anterior
CC process into which the nucleus subsequently translocates. During
CC nucleokinesis dynein at the nuclear surface may translocate the nucleus
CC towards the centrosome by exerting force on centrosomal microtubules.
CC May also play a role in other forms of cell locomotion including the
CC migration of fibroblasts during wound healing. Required for dynein
CC recruitment to microtubule plus ends and BICD2-bound cargos
CC (PubMed:22956769). May modulate the Reelin pathway through interaction
CC of the PAF-AH (I) catalytic dimer with VLDLR (By similarity).
CC {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P63005,
CC ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:22956769}.
CC -!- SUBUNIT: Component of the cytosolic PAF-AH (I) heterotetrameric enzyme,
CC which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and PAFAH1B3
CC (alpha1) subunits. The catalytic activity of the enzyme resides in the
CC alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits, whereas the beta
CC subunit (PAFAH1B1) has regulatory activity. Trimer formation is not
CC essential for the catalytic activity. Interacts with the catalytic
CC dimer of PAF-AH (I) heterotetrameric enzyme: interacts with PAFAH1B2
CC homodimer (alpha2/alpha2 homodimer), PAFAH1B3 homodimer (alpha1/alpha1
CC homodimer) and PAFAH1B2-PAFAH1B3 heterodimer (alpha2/alpha1
CC heterodimer) (By similarity). Interacts with IQGAP1, KATNB1 and NUDC.
CC Interacts with DAB1 when DAB1 is phosphorylated in response to
CC RELN/reelin signaling (By similarity). Can self-associate. Interacts
CC with DCX, dynein, dynactin, NDE1, NDEL1 and RSN. Interacts with DISC1,
CC and this interaction is enhanced by NDEL1. Interacts with INTS13.
CC Interacts with DCDC1 (PubMed:22159412). {ECO:0000250|UniProtKB:P43033,
CC ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:11001923,
CC ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11889140,
CC ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14962739,
CC ECO:0000269|PubMed:14970193, ECO:0000269|PubMed:22159412,
CC ECO:0000269|PubMed:23097494}.
CC -!- INTERACTION:
CC P43034; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-720620, EBI-529989;
CC P43034; P07900: HSP90AA1; NbExp=5; IntAct=EBI-720620, EBI-296047;
CC P43034; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-720620, EBI-928842;
CC P43034; Q8WVJ2: NUDCD2; NbExp=8; IntAct=EBI-720620, EBI-1052153;
CC P43034; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-720620, EBI-744342;
CC P43034; Q9CZA6: Nde1; Xeno; NbExp=6; IntAct=EBI-720620, EBI-309934;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-
CC Rule:MF_03141}. Note=Redistributes to axons during neuronal
CC development. Also localizes to the microtubules of the manchette in
CC elongating spermatids and to the meiotic spindle in spermatocytes (By
CC similarity). Localizes to the plus end of microtubules and to the
CC centrosome. May localize to the nuclear membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43034-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43034-2; Sequence=VSP_019376, VSP_019377, VSP_019378,
CC VSP_019379;
CC -!- TISSUE SPECIFICITY: Fairly ubiquitous expression in both the frontal
CC and occipital areas of the brain.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- DISEASE: Lissencephaly 1 (LIS1) [MIM:607432]: A classical
CC lissencephaly. It is characterized by agyria or pachygyria and
CC disorganization of the clear neuronal lamination of normal six-layered
CC cortex. The cortex is abnormally thick and poorly organized with 4
CC primitive layers. Associated with enlarged and dysmorphic ventricles
CC and often hypoplasia of the corpus callosum.
CC {ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11502906,
CC ECO:0000269|PubMed:15007136, ECO:0000269|PubMed:15173193,
CC ECO:0000269|PubMed:9063735}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Subcortical band heterotopia (SBH) [MIM:607432]: SBH is a mild
CC brain malformation of the lissencephaly spectrum. It is characterized
CC by bilateral and symmetric plates or bands of gray matter found in the
CC central white matter between the cortex and cerebral ventricles,
CC cerebral convolutions usually appearing normal.
CC {ECO:0000269|PubMed:10441340, ECO:0000269|PubMed:14581661}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Miller-Dieker lissencephaly syndrome (MDLS) [MIM:247200]: A
CC contiguous gene deletion syndrome of chromosome 17p13.3, characterized
CC by classical lissencephaly and distinct facial features. Additional
CC congenital malformations can be part of the condition. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Originally the subunits of the type I platelet-
CC activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1),
CC beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity) (Ref.4). Now these
CC subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC alpha1 (PAFAH1B3) respectively (By similarity).
CC {ECO:0000250|UniProtKB:P68402, ECO:0000250|UniProtKB:Q15102,
CC ECO:0000250|UniProtKB:Q29460, ECO:0000303|Ref.4}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02882.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; L13385; AAA02880.1; -; mRNA.
DR EMBL; L13386; AAA02881.1; -; mRNA.
DR EMBL; L13387; AAA02882.1; ALT_SEQ; mRNA.
DR EMBL; U72342; AAC51111.1; -; Genomic_DNA.
DR EMBL; U72334; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72335; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72336; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72337; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72338; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72339; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72340; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; U72341; AAC51111.1; JOINED; Genomic_DNA.
DR EMBL; AF208837; AAL34972.1; -; mRNA.
DR EMBL; AF208838; AAL34973.1; -; mRNA.
DR EMBL; AF400434; AAK92483.1; -; mRNA.
DR EMBL; AK313078; BAG35904.1; -; mRNA.
DR EMBL; BX538346; CAD98141.1; -; mRNA.
DR EMBL; CH471108; EAW90536.1; -; Genomic_DNA.
DR EMBL; BC064638; AAH64638.1; -; mRNA.
DR CCDS; CCDS32528.1; -. [P43034-1]
DR PIR; S36113; S36113.
DR RefSeq; NP_000421.1; NM_000430.3. [P43034-1]
DR RefSeq; XP_016880188.1; XM_017024699.1.
DR RefSeq; XP_016880189.1; XM_017024700.1.
DR RefSeq; XP_016880190.1; XM_017024701.1. [P43034-1]
DR PDB; 7MT1; X-ray; 1.30 A; A=86-410.
DR PDBsum; 7MT1; -.
DR AlphaFoldDB; P43034; -.
DR SMR; P43034; -.
DR BioGRID; 111085; 153.
DR DIP; DIP-35691N; -.
DR IntAct; P43034; 41.
DR MINT; P43034; -.
DR STRING; 9606.ENSP00000380378; -.
DR GlyGen; P43034; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P43034; -.
DR MetOSite; P43034; -.
DR PhosphoSitePlus; P43034; -.
DR SwissPalm; P43034; -.
DR BioMuta; PAFAH1B1; -.
DR DMDM; 1170794; -.
DR CPTAC; CPTAC-103; -.
DR CPTAC; CPTAC-104; -.
DR EPD; P43034; -.
DR jPOST; P43034; -.
DR MassIVE; P43034; -.
DR MaxQB; P43034; -.
DR PaxDb; P43034; -.
DR PeptideAtlas; P43034; -.
DR PRIDE; P43034; -.
DR ProteomicsDB; 55575; -. [P43034-1]
DR ProteomicsDB; 55576; -. [P43034-2]
DR Antibodypedia; 3850; 315 antibodies from 40 providers.
DR DNASU; 5048; -.
DR Ensembl; ENST00000397195.10; ENSP00000380378.4; ENSG00000007168.14. [P43034-1]
DR Ensembl; ENST00000675202.1; ENSP00000502843.1; ENSG00000007168.14. [P43034-1]
DR Ensembl; ENST00000675331.1; ENSP00000502031.1; ENSG00000007168.14. [P43034-1]
DR Ensembl; ENST00000675390.1; ENSP00000501969.1; ENSG00000007168.14. [P43034-1]
DR Ensembl; ENST00000676098.1; ENSP00000502735.1; ENSG00000007168.14. [P43034-1]
DR Ensembl; ENST00000676188.1; ENSP00000502577.1; ENSG00000007168.14. [P43034-1]
DR GeneID; 5048; -.
DR KEGG; hsa:5048; -.
DR MANE-Select; ENST00000397195.10; ENSP00000380378.4; NM_000430.4; NP_000421.1.
DR UCSC; uc002fuw.5; human. [P43034-1]
DR CTD; 5048; -.
DR DisGeNET; 5048; -.
DR GeneCards; PAFAH1B1; -.
DR GeneReviews; PAFAH1B1; -.
DR HGNC; HGNC:8574; PAFAH1B1.
DR HPA; ENSG00000007168; Low tissue specificity.
DR MalaCards; PAFAH1B1; -.
DR MIM; 247200; phenotype.
DR MIM; 601545; gene.
DR MIM; 607432; phenotype.
DR neXtProt; NX_P43034; -.
DR OpenTargets; ENSG00000007168; -.
DR Orphanet; 217385; 17p13.3 microduplication syndrome.
DR Orphanet; 95232; Lissencephaly due to LIS1 mutation.
DR Orphanet; 531; Miller-Dieker syndrome.
DR Orphanet; 99796; Subcortical band heterotopia.
DR PharmGKB; PA32905; -.
DR VEuPathDB; HostDB:ENSG00000007168; -.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR InParanoid; P43034; -.
DR OMA; TQECKCV; -.
DR PhylomeDB; P43034; -.
DR TreeFam; TF105741; -.
DR PathwayCommons; P43034; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P43034; -.
DR SIGNOR; P43034; -.
DR BioGRID-ORCS; 5048; 753 hits in 1086 CRISPR screens.
DR ChiTaRS; PAFAH1B1; human.
DR GeneWiki; PAFAH1B1; -.
DR GenomeRNAi; 5048; -.
DR Pharos; P43034; Tbio.
DR PRO; PR:P43034; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P43034; protein.
DR Bgee; ENSG00000007168; Expressed in sperm and 210 other tissues.
DR ExpressionAtlas; P43034; baseline and differential.
DR Genevisible; P43034; HS.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0000235; C:astral microtubule; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0034452; F:dynactin binding; ISS:BHF-UCL.
DR GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; ISS:BHF-UCL.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0043274; F:phospholipase binding; ISS:BHF-UCL.
DR GO; GO:0051219; F:phosphoprotein binding; ISS:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0001675; P:acrosome assembly; ISS:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:BHF-UCL.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:BHF-UCL.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
DR GO; GO:0060117; P:auditory receptor cell development; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IMP:BHF-UCL.
DR GO; GO:0021987; P:cerebral cortex development; IMP:BHF-UCL.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0021540; P:corpus callosum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0043622; P:cortical microtubule organization; IEA:Ensembl.
DR GO; GO:0051660; P:establishment of centrosome localization; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL.
DR GO; GO:1904936; P:interneuron migration; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISS:BHF-UCL.
DR GO; GO:0007611; P:learning or memory; ISS:BHF-UCL.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051661; P:maintenance of centrosome location; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:BHF-UCL.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007017; P:microtubule-based process; IDA:UniProtKB.
DR GO; GO:0097529; P:myeloid leukocyte migration; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0007405; P:neuroblast proliferation; ISS:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0051081; P:nuclear membrane disassembly; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0046469; P:platelet activating factor metabolic process; ISS:BHF-UCL.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0040019; P:positive regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IEA:Ensembl.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0008090; P:retrograde axonal transport; ISS:BHF-UCL.
DR GO; GO:0017145; P:stem cell division; IEA:Ensembl.
DR GO; GO:0019226; P:transmission of nerve impulse; ISS:BHF-UCL.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:BHF-UCL.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03141; lis1; 1.
DR InterPro; IPR017252; Dynein_regulator_LIS1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF109925; SSF109925; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Disease variant; Lipid degradation; Lipid metabolism;
KW Lissencephaly; Membrane; Microtubule; Mitosis; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..410
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit beta"
FT /id="PRO_0000051061"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 106..147
FT /note="WD 1"
FT REPEAT 148..187
FT /note="WD 2"
FT REPEAT 190..229
FT /note="WD 3"
FT REPEAT 232..271
FT /note="WD 4"
FT REPEAT 274..333
FT /note="WD 5"
FT REPEAT 336..377
FT /note="WD 6"
FT REPEAT 378..410
FT /note="WD 7"
FT REGION 1..102
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 1..66
FT /note="Interaction with NDE1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 1..38
FT /note="Required for self-association and interaction with
FT PAFAH1B2 and PAFAH1B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 83..410
FT /note="Interaction with dynein and dynactin"
FT REGION 367..409
FT /note="Interaction with DCX"
FT /evidence="ECO:0000269|PubMed:11001923"
FT REGION 388..410
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COILED 56..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 12..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019376"
FT VAR_SEQ 134..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019377"
FT VAR_SEQ 237
FT /note="V -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019378"
FT VAR_SEQ 238..410
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019379"
FT VARIANT 31
FT /note="F -> S (in LIS1; dbSNP:rs121434486)"
FT /evidence="ECO:0000269|PubMed:11502906"
FT /id="VAR_015398"
FT VARIANT 149
FT /note="H -> R (in LIS1; abrogates interaction with NDE1 and
FT reduces neuronal migration in vitro; dbSNP:rs121434482)"
FT /evidence="ECO:0000269|PubMed:11163258,
FT ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:9063735"
FT /id="VAR_007724"
FT VARIANT 162
FT /note="G -> S (in LIS1; dbSNP:rs121434487)"
FT /evidence="ECO:0000269|PubMed:11502906"
FT /id="VAR_015399"
FT VARIANT 169
FT /note="S -> P (in SBH; abrogates interaction with NDE1 and
FT reduces neuronal migration in vitro; dbSNP:rs121434484)"
FT /evidence="ECO:0000269|PubMed:10441340,
FT ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:15173193"
FT /id="VAR_010203"
FT VARIANT 241
FT /note="R -> P (in SBH; somatic mosaicism in 18% of
FT lymphocytes and 21% of hair root cells; dbSNP:rs121434488)"
FT /evidence="ECO:0000269|PubMed:14581661"
FT /id="VAR_037300"
FT VARIANT 277
FT /note="H -> P (in LIS1; dbSNP:rs121434490)"
FT /evidence="ECO:0000269|PubMed:15007136"
FT /id="VAR_037301"
FT VARIANT 317
FT /note="D -> H (in LIS1; reduces neuronal migration in
FT vitro; dbSNP:rs121434485)"
FT /evidence="ECO:0000269|PubMed:11502906,
FT ECO:0000269|PubMed:15173193"
FT /id="VAR_015400"
FT CONFLICT 21
FT /note="S -> P (in Ref. 3; AAL34972/AAL34973)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="E -> G (in Ref. 3; AAL34973)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="W -> R (in Ref. 3; AAL34973)"
FT /evidence="ECO:0000305"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:7MT1"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:7MT1"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:7MT1"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:7MT1"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:7MT1"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7MT1"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:7MT1"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:7MT1"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 390..399
FT /evidence="ECO:0007829|PDB:7MT1"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:7MT1"
SQ SEQUENCE 410 AA; 46638 MW; 3AB68D2641BA31C9 CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK
TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
