LIS1_MOUSE
ID LIS1_MOUSE Reviewed; 410 AA.
AC P63005; O35592; P43035; P81692; Q9R2A6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
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:0000312|MGI:MGI:109520}; Synonyms=Lis-1, Lis1, Pafaha;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=7821822; DOI=10.1016/0378-1119(94)90468-5;
RA Peterfy M., Gyuris T., Basu R., Takacs L.;
RT "Lissencephaly-1 is one of the most conserved proteins between mouse and
RT human: a single amino-acid difference in 410 residues.";
RL Gene 150:415-416(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=9479492; DOI=10.1006/geno.1997.5121;
RA Peterfy M., Gyuris T., Grosshans D., Cuaresma C.C., Takacs L.;
RT "Cloning and characterization of cDNAs and the gene encoding the mouse
RT platelet-activating factor acetylhydrolase Ib alpha subunit/lissencephaly-1
RT protein.";
RL Genomics 47:200-206(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-410 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7751941; DOI=10.1523/jneurosci.15-05-03730.1995;
RA Reiner O., Albrecht U., Gordon M., Chianese K.A., Carrozzo R., Wong C.,
RA Lindsay E.A., Siracusa L.D., Baldini A., Ledbetter D.H., Eichele G.,
RA Buchberg A.M., Caskey T.C.;
RT "Lissencephaly gene (LIS1) expression in the CNS suggests a role in
RT neuronal migration.";
RL J. Neurosci. 15:3730-3738(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=11756344; DOI=10.2337/diabetes.51.1.215;
RA Grattan M., Mi Q.-S., Meagher C., Delovitch T.L.;
RT "Congenic mapping of the diabetogenic locus Idd4 to a 5.2-cM region of
RT chromosome 11 in NOD mice: identification of two potential candidate
RT subloci.";
RL Diabetes 51:215-223(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Eye, and Mammary tumor;
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 [6]
RP PROTEIN SEQUENCE OF 133-144 AND 375-405, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP INTERACTION WITH DCX, AND DEVELOPMENTAL STAGE.
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 [8]
RP FUNCTION, INTERACTION WITH DYNEIN AND DYNACTIN, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11056530; DOI=10.1038/35041000;
RA Smith D.S., Niethammer M., Ayala R., Zhou Y., Gambello M.J.,
RA Wynshaw-Boris A., Tsai L.-H.;
RT "Regulation of cytoplasmic dynein behaviour and microtubule organization by
RT mammalian Lis1.";
RL Nat. Cell Biol. 2:767-775(2000).
RN [9]
RP INTERACTION WITH NDE1.
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 [10]
RP SELF-ASSOCIATION, INTERACTION WITH DYNEIN AND NDEL1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF HIS-149.
RX PubMed=11163259; DOI=10.1016/s0896-6273(00)00146-x;
RA Sasaki S., Shionoya A., Ishida M., Gambello M.J., Yingling J.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing and
RT adult nervous system.";
RL Neuron 28:681-696(2000).
RN [11]
RP INTERACTION WITH NDEL1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11163260; DOI=10.1016/s0896-6273(00)00147-1;
RA Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
RA Morabito M., Tsai L.-H.;
RT "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic
RT dynein.";
RL Neuron 28:697-711(2000).
RN [12]
RP INTERACTION WITH NDEL1, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF HIS-149;
RP SER-152 AND SER-169.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11231056; DOI=10.1016/s0925-4773(00)00543-8;
RA Sweeney K.J., Prokscha A., Eichele G.;
RT "NudE-L, a novel Lis1-interacting protein, belongs to a family of
RT vertebrate coiled-coil proteins.";
RL Mech. Dev. 101:21-33(2001).
RN [13]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH PAFAH1B2 AND PAFAH1B3, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11344260; DOI=10.1073/pnas.101122598;
RA Cahana A., Escamez T., Nowakowski R.S., Hayes N.L., Giacobini M.,
RA von Holst A., Shmueli O., Sapir T., McConnell S.K., Wurst W., Martinez S.,
RA Reiner O.;
RT "Targeted mutagenesis of Lis1 disrupts cortical development and LIS1
RT homodimerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6429-6434(2001).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RSN.
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 [15]
RP FUNCTION.
RX PubMed=12911752; DOI=10.1046/j.1460-9568.2003.02778.x;
RA Tokuoka S.M., Ishii S., Kawamura N., Satoh M., Shimada A., Sasaki S.,
RA Hirotsune S., Wynshaw-Boris A., Shimizu T.;
RT "Involvement of platelet-activating factor and LIS1 in neuronal
RT migration.";
RL Eur. J. Neurosci. 18:563-570(2003).
RN [16]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12551946; DOI=10.1074/jbc.m211836200;
RA Koizumi H., Yamaguchi N., Hattori M., Ishikawa T., Aoki J., Taketo M.M.,
RA Inoue K., Arai H.;
RT "Targeted disruption of intracellular type I platelet activating factor-
RT acetylhydrolase catalytic subunits causes severe impairment in
RT spermatogenesis.";
RL J. Biol. Chem. 278:12489-12494(2003).
RN [17]
RP SELF-ASSOCIATION, INTERACTION WITH NUDC; NDE1; NDEL1; PAFAH1B2; PAFAH1B3
RP AND RSN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-31; HIS-149; GLY-162;
RP SER-169 AND ASP-317.
RX PubMed=12885786; DOI=10.1074/jbc.m301147200;
RA Caspi M., Coquelle F.M., Koifman C., Levy T., Arai H., Aoki J.,
RA De Mey J.R., Reiner O.;
RT "LIS1 missense mutations: variable phenotypes result from unpredictable
RT alterations in biochemical and cellular properties.";
RL J. Biol. Chem. 278:38740-38748(2003).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14691133; DOI=10.1083/jcb.200310097;
RA Dujardin D.L., Barnhart L.E., Stehman S.A., Gomes E.R., Gundersen G.G.,
RA Vallee R.B.;
RT "A role for cytoplasmic dynein and LIS1 in directed cell movement.";
RL J. Cell Biol. 163:1205-1211(2003).
RN [19]
RP FUNCTION.
RX PubMed=14507966; DOI=10.1523/jneurosci.23-25-08673.2003;
RA Kholmanskikh S.S., Dobrin J.S., Wynshaw-Boris A., Letourneau P.C.,
RA Ross M.E.;
RT "Disregulated RhoGTPases and actin cytoskeleton contribute to the migration
RT defect in Lis1-deficient neurons.";
RL J. Neurosci. 23:8673-8681(2003).
RN [20]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12950100; DOI=10.1002/mrd.10339;
RA Cahana A., Jin X.L., Reiner O., Wynshaw-Boris A., O'Neill C.;
RT "A study of the nature of embryonic lethality in LIS1-/- mice.";
RL Mol. Reprod. Dev. 66:134-142(2003).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12796778; DOI=10.1038/ng1169;
RA Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
RA Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D., Hirotsune S.,
RA Wynshaw-Boris A.;
RT "14-3-3epsilon is important for neuronal migration by binding to NUDEL: a
RT molecular explanation for Miller-Dieker syndrome.";
RL Nat. Genet. 34:274-285(2003).
RN [22]
RP FUNCTION, INTERACTION WITH DAB1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-149.
RX PubMed=14578885; DOI=10.1038/ng1257;
RA Assadi A.H., Zhang G., Beffert U., McNeil R.S., Renfro A.L., Niu S.,
RA Quattrocchi C.C., Antalffy B.A., Sheldon M., Armstrong D.D.,
RA Wynshaw-Boris A., Herz J., D'Arcangelo G., Clark G.D.;
RT "Interaction of reelin signaling and Lis1 in brain development.";
RL Nat. Genet. 35:270-276(2003).
RN [23]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15147871; DOI=10.1016/j.febslet.2004.04.009;
RA Yamaguchi N., Takanezawa Y., Koizumi H., Umezu-Goto M., Aoki J., Arai H.;
RT "Expression of NUDEL in manchette and its implication in spermatogenesis.";
RL FEBS Lett. 566:71-76(2004).
RN [24]
RP FUNCTION, INTERACTION WITH DYNEIN AND DCX, AND SUBCELLULAR LOCATION.
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 [25]
RP FUNCTION, INTERACTION WITH DYNEIN AND DCX, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15473966; DOI=10.1016/j.neuron.2004.09.030;
RA Shu T., Ayala R., Nguyen M.-D., Xie Z., Gleeson J.G., Tsai L.-H.;
RT "Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to
RT regulate cortical neuronal positioning.";
RL Neuron 44:263-277(2004).
RN [26]
RP INTERACTION WITH NDE1.
RX PubMed=15473967; DOI=10.1016/j.neuron.2004.09.023;
RA Feng Y., Walsh C.A.;
RT "Mitotic spindle regulation by Nde1 controls cerebral cortical size.";
RL Neuron 44:279-293(2004).
RN [27]
RP SELF-ASSOCIATION, DOMAIN, AND MUTAGENESIS OF ILE-15 AND LEU-19.
RX PubMed=16258276; DOI=10.4161/cc.4.11.2151;
RA Gerlitz G., Darhin E., Giorgio G., Franco B., Reiner O.;
RT "Novel functional features of the Lis-H domain: role in protein
RT dimerization, half-life and cellular localization.";
RL Cell Cycle 4:1632-1640(2005).
RN [28]
RP FUNCTION, AND INTERACTION WITH KATNB1.
RX PubMed=16203747; DOI=10.1093/hmg/ddi339;
RA Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T., Toyoshima Y.Y.,
RA Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M., Hiraiwa N., Yoshiki A.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting
RT protein, is essential for mitotic cell division and neuronal migration.";
RL Hum. Mol. Genet. 14:3113-3128(2005).
RN [29]
RP FUNCTION.
RX PubMed=16107726; DOI=10.1128/mcb.25.17.7812-7827.2005;
RA Sasaki S., Mori D., Toyo-oka K., Chen A., Garrett-Beal L., Muramatsu M.,
RA Miyagawa S., Hiraiwa N., Yoshiki A., Wynshaw-Boris A., Hirotsune S.;
RT "Complete loss of Ndel1 results in neuronal migration defects and early
RT embryonic lethality.";
RL Mol. Cell. Biol. 25:7812-7827(2005).
RN [30]
RP SUBCELLULAR LOCATION.
RX PubMed=15939891; DOI=10.1073/pnas.0502303102;
RA Soukoulis V., Reddy S., Pooley R.D., Feng Y., Walsh C.A., Bader D.M.;
RT "Cytoplasmic LEK1 is a regulator of microtubule function through its
RT interaction with the LIS1 pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8549-8554(2005).
RN [31]
RP FUNCTION, AND INTERACTION WITH DYNEIN AND PAFAH1B2.
RX PubMed=16481446; DOI=10.1523/jneurosci.5095-05.2006;
RA Mesngon M.T., Tarricone C., Hebbar S., Guillotte A.M., Schmitt E.W.,
RA Lanier L., Musacchio A., King S.J., Smith D.S.;
RT "Regulation of cytoplasmic dynein ATPase by Lis1.";
RL J. Neurosci. 26:2132-2139(2006).
RN [32]
RP INTERACTION WITH NDEL1, AND SUBCELLULAR LOCATION.
RX PubMed=16291865; DOI=10.1091/mbc.e05-04-0360;
RA Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.;
RT "Nudel contributes to microtubule anchoring at the mother centriole and is
RT involved in both dynein-dependent and -independent centrosomal protein
RT assembly.";
RL Mol. Biol. Cell 17:680-689(2006).
RN [33]
RP FUNCTION, AND INTERACTION WITH IQGAP1 AND RSN.
RX PubMed=16369480; DOI=10.1038/nn1619;
RA Kholmanskikh S.S., Koeller H.B., Wynshaw-Boris A., Gomez T.,
RA Letourneau P.C., Ross M.E.;
RT "Calcium-dependent interaction of Lis1 with IQGAP1 and Cdc42 promotes
RT neuronal motility.";
RL Nat. Neurosci. 9:50-57(2006).
RN [34]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17330141; DOI=10.1371/journal.pone.0000252;
RA Zhang G., Assadi A.H., McNeil R.S., Beffert U., Wynshaw-Boris A., Herz J.,
RA Clark G.D., D'Arcangelo G.;
RT "The Pafah1b complex interacts with the reelin receptor VLDLR.";
RL PLoS ONE 2:e252-e252(2007).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [36]
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 [37]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH PAFAH1B2, INTERACTION
RP WITH NDEL1, AND MUTAGENESIS OF ARG-238.
RX PubMed=15572112; DOI=10.1016/j.neuron.2004.11.019;
RA Tarricone C., Perrina F., Monzani S., Massimiliano L., Kim M.-H.,
RA Derewenda Z.S., Knapp S., Tsai L.-H., Musacchio A.;
RT "Coupling PAF signaling to dynein regulation: structure of LIS1 in complex
RT with PAF-acetylhydrolase.";
RL Neuron 44:809-821(2004).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-86, DOMAIN, AND CIRCULAR
RP DICHROISM ANALYSIS.
RX PubMed=15274919; DOI=10.1016/j.str.2004.03.024;
RA Kim M.-H., Cooper D.R., Oleksy A., Devedjiev Y., Derewenda U., Reiner O.,
RA Otlewski J., Derewenda Z.S.;
RT "The structure of the N-terminal domain of the product of the lissencephaly
RT gene Lis1 and its functional implications.";
RL Structure 12:987-998(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). Positively regulates the activity of
CC the minus-end directed microtubule motor protein dynein. May enhance
CC dynein-mediated microtubule sliding by targeting dynein to the
CC microtubule plus end. Required for several dynein- and microtubule-
CC dependent processes such as the maintenance of Golgi integrity, the
CC peripheral transport of microtubule fragments and the coupling of the
CC nucleus and centrosome. Required during brain development for the
CC proliferation of neuronal precursors and the migration of newly formed
CC neurons from the ventricular/subventricular zone toward the cortical
CC plate. Neuronal migration involves a process called nucleokinesis,
CC whereby migrating cells extend an anterior process into which the
CC nucleus subsequently translocates. During nucleokinesis dynein at the
CC nuclear surface may translocate the nucleus towards the centrosome by
CC exerting force on centrosomal microtubules. Also required for proper
CC activation of Rho GTPases and actin polymerization at the leading edge
CC of locomoting cerebellar neurons and postmigratory hippocampal neurons
CC in response to calcium influx triggered via NMDA receptors. May also
CC play a role in other forms of cell locomotion including the migration
CC of fibroblasts during wound healing. Non-catalytic subunit of an
CC acetylhydrolase complex which inactivates platelet-activating factor
CC (PAF) by removing the acetyl group at the SN-2 position. Required for
CC dynein recruitment to microtubule plus ends and BICD2-bound cargos (By
CC similarity). May modulate the Reelin pathway through interaction of the
CC PAF-AH (I) catalytic dimer with VLDLR (PubMed:17330141).
CC {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034,
CC ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11056530,
CC ECO:0000269|PubMed:11344260, ECO:0000269|PubMed:12796778,
CC ECO:0000269|PubMed:12911752, ECO:0000269|PubMed:14507966,
CC ECO:0000269|PubMed:14578885, ECO:0000269|PubMed:14691133,
CC ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:15473966,
CC ECO:0000269|PubMed:16107726, ECO:0000269|PubMed:16203747,
CC ECO:0000269|PubMed:16369480, ECO:0000269|PubMed:16481446,
CC ECO:0000269|PubMed:17330141}.
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) (PubMed:11344260, PubMed:12885786, PubMed:16481446). Can
CC self-associate (PubMed:11163259, PubMed:11344260, PubMed:12885786,
CC PubMed:15572112). Interacts with DCX, dynein, dynactin, IQGAP1, KATNB1,
CC NDE1, NDEL1, NUDC, and RSN (PubMed:11001923, PubMed:11056530,
CC PubMed:11163258, PubMed:11163259, PubMed:11163260, PubMed:11231056,
CC PubMed:11940666, PubMed:12885786, PubMed:15173193, PubMed:15473966,
CC PubMed:15473967, PubMed:15572112, PubMed:16203747, PubMed:16291865,
CC PubMed:16481446, PubMed:16369480). Interacts with DAB1 when DAB1 is
CC phosphorylated in response to RELN/reelin signaling (PubMed:14578885).
CC Interacts with INTS13 (PubMed:23097494). Interacts with DCDC1 (By
CC similarity). Interacts with DISC1, and this interaction is enhanced by
CC NDEL1 (By similarity). {ECO:0000250|UniProtKB:P43034,
CC ECO:0000269|PubMed:11001923, ECO:0000269|PubMed:11056530,
CC ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11163259,
CC ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056,
CC ECO:0000269|PubMed:11344260, ECO:0000269|PubMed:11940666,
CC ECO:0000269|PubMed:12885786, ECO:0000269|PubMed:14578885,
CC ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:15473966,
CC ECO:0000269|PubMed:15473967, ECO:0000269|PubMed:15572112,
CC ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:16291865,
CC ECO:0000269|PubMed:16369480, ECO:0000269|PubMed:16481446,
CC ECO:0000269|PubMed:23097494}.
CC -!- INTERACTION:
CC P63005; Q9ERR1: Ndel1; NbExp=9; IntAct=EBI-917499, EBI-646668;
CC P63005; Q61205: Pafah1b3; NbExp=2; IntAct=EBI-917499, EBI-1007637;
CC P63005; Q9GZM8: NDEL1; Xeno; NbExp=4; IntAct=EBI-917499, EBI-928842;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Cytoplasm, cytoskeleton,
CC spindle. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=May
CC localize to the nuclear membrane (By similarity). Localizes to the plus
CC end of microtubules and to the centrosome. Redistributes to axons
CC during neuronal development. Also localizes to the microtubules of the
CC manchette in elongating spermatids and to the meiotic spindle in
CC spermatocytes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63005-1, P43035-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P63005-2, P43035-2;
CC Sequence=VSP_006778;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, particularly the
CC hippocampus and the olfactory bulb. Also highly expressed in testis,
CC including all seminiferous tubule cell types, all types of
CC spermatogenic and Sertoli cells, and meiotically dividing and
CC elongating spermatids. Expressed at lower levels in heart, kidney,
CC large intestine, liver, lung, ovary, small intestine and spleen.
CC {ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:11163260,
CC ECO:0000269|PubMed:12551946}.
CC -!- DEVELOPMENTAL STAGE: Embryonic expression begins prior to the
CC blastocyst stage, when maternally expressed protein is depleted. By
CC 10.5 dpc, expression is abundant in the developing central and
CC peripheral nervous systems. Major sites of expression include the
CC neuroepithelium of the fore-, mid-, and hindbrain, the spinal cord, the
CC dorsal root and the cranial ganglia. By 13.5 dpc, highly expressed in
CC neuroblasts as well as postmitotic neurons of the cortical plate. After
CC completion of neuronal migration expression remains high in the cortex.
CC Also expressed in the testis from P8. {ECO:0000269|PubMed:11001923,
CC ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:11163259,
CC ECO:0000269|PubMed:11231056, ECO:0000269|PubMed:11344260,
CC ECO:0000269|PubMed:12950100, ECO:0000269|PubMed:15147871,
CC ECO:0000269|PubMed:15473966}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141,
CC ECO:0000269|PubMed:15274919, ECO:0000269|PubMed:16258276}.
CC -!- DISRUPTION PHENOTYPE: Double heterozygous PAFAH1B1 and homozygous VLDLR
CC knockout mice present no obvious cortical layering defects
CC (PubMed:17330141). Double heterozygous PAFAH1B1 and homozygous LRP8
CC knockout mice display a reeler-like phenotype in the forebrain
CC consisting of the inversion of cortical layers and hippocampal
CC disorganization (PubMed:17330141). {ECO:0000269|PubMed:17330141}.
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). Now these
CC subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC alpha1 (PAFAH1B3) respectively (By similarity).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC ECO:0000250|UniProtKB:Q15102, ECO:0000250|UniProtKB:Q29460}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
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DR EMBL; U95116; AAC04610.1; -; mRNA.
DR EMBL; U95120; AAC63099.1; -; Genomic_DNA.
DR EMBL; U95119; AAC63099.1; JOINED; Genomic_DNA.
DR EMBL; U95120; AAC63098.1; -; Genomic_DNA.
DR EMBL; U95119; AAC63098.1; JOINED; Genomic_DNA.
DR EMBL; L25109; AAD23059.1; -; mRNA.
DR EMBL; AY189217; AAO41716.1; -; mRNA.
DR EMBL; AY189218; AAO41717.1; -; mRNA.
DR EMBL; BC014831; AAH14831.1; -; mRNA.
DR EMBL; BC026141; AAH26141.1; -; mRNA.
DR CCDS; CCDS25035.1; -.
DR RefSeq; NP_038653.1; NM_013625.4. [P63005-1]
DR PDB; 1UUJ; X-ray; 1.75 A; A/B/C/D=1-86.
DR PDB; 1VYH; X-ray; 3.40 A; C/D/G/H/K/L/O/P/S/T=1-410.
DR PDBsum; 1UUJ; -.
DR PDBsum; 1VYH; -.
DR AlphaFoldDB; P63005; -.
DR SMR; P63005; -.
DR BioGRID; 202013; 73.
DR DIP; DIP-29555N; -.
DR IntAct; P63005; 41.
DR MINT; P63005; -.
DR STRING; 10090.ENSMUSP00000021091; -.
DR iPTMnet; P63005; -.
DR PhosphoSitePlus; P63005; -.
DR SwissPalm; P63005; -.
DR REPRODUCTION-2DPAGE; P63005; -.
DR EPD; P63005; -.
DR jPOST; P63005; -.
DR MaxQB; P63005; -.
DR PaxDb; P63005; -.
DR PeptideAtlas; P63005; -.
DR PRIDE; P63005; -.
DR ProteomicsDB; 292334; -.
DR ProteomicsDB; 292335; -. [P63005-2]
DR Antibodypedia; 3850; 315 antibodies from 40 providers.
DR DNASU; 18472; -.
DR Ensembl; ENSMUST00000021091; ENSMUSP00000021091; ENSMUSG00000020745. [P63005-1]
DR Ensembl; ENSMUST00000102520; ENSMUSP00000099578; ENSMUSG00000020745. [P63005-1]
DR GeneID; 18472; -.
DR KEGG; mmu:18472; -.
DR UCSC; uc007kce.2; mouse.
DR CTD; 5048; -.
DR MGI; MGI:109520; Pafah1b1.
DR VEuPathDB; HostDB:ENSMUSG00000020745; -.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; P63005; -.
DR OMA; TQECKCV; -.
DR PhylomeDB; P63005; -.
DR TreeFam; TF105741; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 18472; 24 hits in 70 CRISPR screens.
DR ChiTaRS; Pafah1b1; mouse.
DR EvolutionaryTrace; P63005; -.
DR PRO; PR:P63005; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63005; protein.
DR Bgee; ENSMUSG00000020745; Expressed in seminiferous tubule of testis and 299 other tissues.
DR ExpressionAtlas; P63005; baseline and differential.
DR Genevisible; P63005; MM.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0000235; C:astral microtubule; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0090724; C:central region of growth cone; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005875; C:microtubule associated complex; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0001667; P:ameboidal-type cell migration; IMP:MGI.
DR GO; GO:0060117; P:auditory receptor cell development; IMP:CACAO.
DR GO; GO:0048854; P:brain morphogenesis; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:CACAO.
DR GO; GO:0021540; P:corpus callosum morphogenesis; ISO:MGI.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:CACAO.
DR GO; GO:0051660; P:establishment of centrosome localization; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IMP:CACAO.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:1904936; P:interneuron migration; IMP:MGI.
DR GO; GO:0007254; P:JNK cascade; IGI:MGI.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IGI:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IMP:CACAO.
DR GO; GO:0031023; P:microtubule organizing center organization; ISO:MGI.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007017; P:microtubule-based process; ISO:MGI.
DR GO; GO:0097529; P:myeloid leukocyte migration; IMP:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0051081; P:nuclear membrane disassembly; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; ISO:MGI.
DR GO; GO:0036035; P:osteoclast development; IMP:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0051130; P:positive regulation of cellular component organization; IMP:CACAO.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:CACAO.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:CACAO.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0009306; P:protein secretion; IMP:MGI.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IGI:MGI.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:CACAO.
DR GO; GO:0008090; P:retrograde axonal transport; IDA:MGI.
DR GO; GO:0017145; P:stem cell division; ISO:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
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; Direct protein sequencing; Lipid degradation;
KW Lipid metabolism; 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_0000051063"
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 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 REGION 83..410
FT /note="Interaction with dynein and dynactin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 367..409
FT /note="Interaction with DCX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 388..410
FT /note="Interaction with NDEL1"
FT COILED 56..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43034"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43034"
FT VAR_SEQ 387..410
FT /note="DFHKTAPYVVTGSVDQTVKVWECR -> GMYTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7751941"
FT /id="VSP_006778"
FT MUTAGEN 15
FT /note="I->R: Impairs self-association and reduces protein
FT stability."
FT /evidence="ECO:0000269|PubMed:16258276"
FT MUTAGEN 19
FT /note="L->R: Impairs self-association, reduces protein
FT stability and promotes localization to actin fibers."
FT /evidence="ECO:0000269|PubMed:16258276"
FT MUTAGEN 31
FT /note="F->S: Abrogates interaction with NDLE1, NUDC,
FT PAFAH1B3 and RSN. Also impairs localization to centrosomes
FT and microtubule plus ends. Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:12885786"
FT MUTAGEN 149
FT /note="H->R: Abrogates self-association and interaction
FT with DAB1, dynein, NDEL1, PAFAH1B3 and RSN. Also impairs
FT localization to centrosomes and microtubule plus ends.
FT Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:11163259,
FT ECO:0000269|PubMed:11231056, ECO:0000269|PubMed:12885786,
FT ECO:0000269|PubMed:14578885"
FT MUTAGEN 152
FT /note="S->W: Abrogates interaction with NDEL1."
FT /evidence="ECO:0000269|PubMed:11231056"
FT MUTAGEN 162
FT /note="G->S: Abrogates interaction with PAFAH1B3 and RSN.
FT Also impairs localization to centrosomes and microtubule
FT plus ends. Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:12885786"
FT MUTAGEN 169
FT /note="S->P: Abrogates interaction with NDEL1, PAFAH1B3 and
FT RSN. Also impairs localization to centrosomes and
FT microtubule plus ends. Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:11231056,
FT ECO:0000269|PubMed:12885786"
FT MUTAGEN 238
FT /note="R->A: Abrogates interaction with PAFAH1B2."
FT /evidence="ECO:0000269|PubMed:15572112"
FT MUTAGEN 317
FT /note="D->H: Abrogates interaction with NDEL1, PAFAH1B3 and
FT RSN. Also impairs localization to centrosomes and
FT microtubule plus ends. Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:12885786"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:1UUJ"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1UUJ"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:1UUJ"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:1UUJ"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:1UUJ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1VYH"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1VYH"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1VYH"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:1VYH"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:1VYH"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1VYH"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:1VYH"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:1VYH"
SQ SEQUENCE 410 AA; 46670 MW; 4DBF6A24A6B131CD CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN 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
