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 22-FEB-2023, entry version 221. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 176. DR DIP; DIP-35691N; -. DR IntAct; P43034; 47. 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 ProteomicsDB; 55575; -. [P43034-1] DR ProteomicsDB; 55576; -. [P43034-2] DR Antibodypedia; 3850; 318 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 AGR; HGNC:8574; -. 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 OrthoDB; 1798470at2759; -. 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; 790 hits in 1166 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:0098978; C:glutamatergic synapse; IEA:Ensembl. 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:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0032420; C:stereocilium; IEA:Ensembl. 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:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl. 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 CDD; cd00200; WD40; 1. DR Gene3D; 1.20.960.30; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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 PANTHER; PTHR44129:SF16; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA; 1. DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1. 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; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 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 //