DPYL1_HUMAN
ID DPYL1_HUMAN Reviewed; 572 AA.
AC Q14194; A0EJG6; Q13024; Q4W5F1; Q96TC8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Dihydropyrimidinase-related protein 1;
DE Short=DRP-1;
DE AltName: Full=Collapsin response mediator protein 1;
DE Short=CRMP-1;
DE AltName: Full=Inactive dihydropyrimidinase {ECO:0000305};
DE AltName: Full=Unc-33-like phosphoprotein 3;
DE Short=ULIP-3;
GN Name=CRMP1; Synonyms=DPYSL1, ULIP3;
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;
RX PubMed=8973361; DOI=10.1016/s0378-1119(96)00445-3;
RA Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.;
RT "A novel gene family defined by human dihydropyrimidinase and three related
RT proteins with differential tissue distribution.";
RL Gene 180:157-163(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-1), AND ALTERNATIVE SPLICING.
RC TISSUE=Lung adenocarcinoma;
RX PubMed=19362386; DOI=10.1016/j.lungcan.2009.03.006;
RA Pan S.-H., Chao Y.-C., Chen H.Y., Hung P.F., Lin P.Y., Lin C.W.,
RA Chang Y.L., Wu C.T., Lee Y.C., Yang S.-C., Hong T.-M., Yang P.-C.;
RT "Long form collapsin response mediator protein-1 (LCRMP-1) expression is
RT associated with clinical outcome and lymph node metastasis in non-small
RT cell lung cancer patients.";
RL Lung Cancer 67:93-100(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-572 (ISOFORM 1).
RX PubMed=10048489; DOI=10.1093/dnares/5.6.393;
RA Torres R., Polymeropoulos M.H.;
RT "Genomic organization and localization of the human CRMP-1 gene.";
RL DNA Res. 5:393-395(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-572 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7637782; DOI=10.1038/376509a0;
RA Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.;
RT "Collapsin-induced growth cone collapse mediated by an intracellular
RT protein related to UNC-33.";
RL Nature 376:509-514(1995).
RN [9]
RP PROTEIN SEQUENCE OF 44-56; 190-210; 246-254; 259-268; 346-361; 391-397;
RP 452-463; 472-481; 488-511 AND 533-552, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP SUBUNIT, AND INTERACTION WITH DPYSL2 AND DPYSL4.
RX PubMed=9375656; DOI=10.1046/j.1471-4159.1997.69062261.x;
RA Wang L.H., Strittmatter S.M.;
RT "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase.";
RL J. Neurochem. 69:2261-2269(1997).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11562390; DOI=10.1093/jnci/93.18.1392;
RA Shih J.-Y., Yang S.-C., Hong T.-M., Yuan A., Chen J.J.W., Yu C.-J.,
RA Chang Y.-L., Lee Y.-C., Peck K., Wu C.-W., Yang P.-C.;
RT "Collapsin response mediator protein-1 and the invasion and metastasis of
RT cancer cells.";
RL J. Natl. Cancer Inst. 93:1392-1400(2001).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT THR-101 AND THR-102, AND MUTAGENESIS OF
RP 101-THR-THR-102.
RX PubMed=19799413; DOI=10.1021/pr900325f;
RA Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C.,
RA Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.;
RT "From midbody protein-protein interaction network construction to novel
RT regulators in cytokinesis.";
RL J. Proteome Res. 8:4943-4953(2009).
RN [13]
RP FUNCTION, INTERACTION WITH FLNA, MOTIF, AND PHOSPHORYLATION AT SER-522.
RX PubMed=25358863; DOI=10.1038/ncomms6325;
RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA Mitani S., Ogino T., Goshima Y.;
RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT mediate Sema3A signalling.";
RL Nat. Commun. 5:5325-5325(2014).
RN [14] {ECO:0007744|PDB:4B3Z}
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS).
RX PubMed=26249678; DOI=10.1107/s2053230x15009243;
RA Liu S.H., Huang S.F., Hsu Y.L., Pan S.H., Chen Y.J., Lin Y.H.;
RT "Structure of human collapsin response mediator protein 1: a possible role
RT of its C-terminal tail.";
RL Acta Crystallogr. F 71:938-945(2015).
CC -!- FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent
CC remodeling of the cytoskeleton (PubMed:25358863). Plays a role in axon
CC guidance (PubMed:25358863). During the axon guidance process, acts
CC downstream of SEMA3A to promote FLNA dissociation from F-actin which
CC results in the rearrangement of the actin cytoskeleton and the collapse
CC of the growth cone (PubMed:25358863). Involved in invasive growth and
CC cell migration (PubMed:11562390). May participate in cytokinesis
CC (PubMed:19799413). {ECO:0000269|PubMed:11562390,
CC ECO:0000269|PubMed:19799413, ECO:0000269|PubMed:25358863}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4
CC or DPYSL5 (By similarity). Interacts with PLXNA1 (By similarity).
CC Interacts with FLNA (via calponin-homology (CH) domain 1 and filamin
CC repeat 24); the interaction alters FLNA ternary structure and thus
CC promotes FLNA dissociation from F-actin (PubMed:25358863).
CC {ECO:0000250|UniProtKB:P97427, ECO:0000269|PubMed:25358863}.
CC -!- INTERACTION:
CC Q14194; Q9Y2T2: AP3M1; NbExp=6; IntAct=EBI-473101, EBI-2371151;
CC Q14194; O15169: AXIN1; NbExp=2; IntAct=EBI-473101, EBI-710484;
CC Q14194; P23560-2: BDNF; NbExp=3; IntAct=EBI-473101, EBI-12275524;
CC Q14194; Q14194: CRMP1; NbExp=3; IntAct=EBI-473101, EBI-473101;
CC Q14194; P02511: CRYAB; NbExp=3; IntAct=EBI-473101, EBI-739060;
CC Q14194; Q16555: DPYSL2; NbExp=5; IntAct=EBI-473101, EBI-1104711;
CC Q14194; Q14195-2: DPYSL3; NbExp=6; IntAct=EBI-473101, EBI-10232496;
CC Q14194; P04406: GAPDH; NbExp=3; IntAct=EBI-473101, EBI-354056;
CC Q14194; P07900: HSP90AA1; NbExp=3; IntAct=EBI-473101, EBI-296047;
CC Q14194; P42858: HTT; NbExp=14; IntAct=EBI-473101, EBI-466029;
CC Q14194; P63244: RACK1; NbExp=3; IntAct=EBI-473101, EBI-296739;
CC Q14194; P08670: VIM; NbExp=3; IntAct=EBI-473101, EBI-353844;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562390}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:11562390}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:11562390}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P97427}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P97427}. Perikaryon
CC {ECO:0000250|UniProtKB:P97427}. Note=Associated with centrosomes and
CC the mitotic spindle during metaphase (PubMed:11562390). Colocalizes
CC with FLNA and tubulin in the central region of DRG neuron growth cone
CC (By similarity). Following SEMA3A stimulation of DRG neurons,
CC colocalizes with F-actin (By similarity).
CC {ECO:0000250|UniProtKB:P97427, ECO:0000269|PubMed:11562390}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14194-1; Sequence=Displayed;
CC Name=LCRMP-1;
CC IsoId=Q14194-2; Sequence=VSP_042545;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- PTM: Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of
CC FLNA ternary structure and FLNA dissociation from F-actin.
CC {ECO:0000269|PubMed:25358863}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC -!- CAUTION: Lacks most of the conserved residues that are essential for
CC binding the metal cofactor and hence for dihydropyrimidinase activity.
CC Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR EMBL; D78012; BAA11190.1; -; mRNA.
DR EMBL; DQ206871; ABB22046.1; -; mRNA.
DR EMBL; BT006806; AAP35452.1; -; mRNA.
DR EMBL; AC105915; AAY40959.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82405.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82407.1; -; Genomic_DNA.
DR EMBL; BC000252; AAH00252.1; -; mRNA.
DR EMBL; BC007613; AAH07613.1; -; mRNA.
DR EMBL; AH010780; AAK55500.1; -; Genomic_DNA.
DR EMBL; U17278; AAA93201.1; -; mRNA.
DR CCDS; CCDS33950.1; -. [Q14194-2]
DR CCDS; CCDS43207.1; -. [Q14194-1]
DR PIR; JC5316; JC5316.
DR RefSeq; NP_001014809.1; NM_001014809.2. [Q14194-2]
DR RefSeq; NP_001275590.1; NM_001288661.1.
DR RefSeq; NP_001275591.1; NM_001288662.1.
DR RefSeq; NP_001304.1; NM_001313.4. [Q14194-1]
DR PDB; 4B3Z; X-ray; 3.05 A; A/B/C/D=1-572.
DR PDBsum; 4B3Z; -.
DR AlphaFoldDB; Q14194; -.
DR SMR; Q14194; -.
DR BioGRID; 107790; 124.
DR CORUM; Q14194; -.
DR IntAct; Q14194; 93.
DR MINT; Q14194; -.
DR STRING; 9606.ENSP00000321606; -.
DR MEROPS; M38.974; -.
DR GlyGen; Q14194; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14194; -.
DR PhosphoSitePlus; Q14194; -.
DR SwissPalm; Q14194; -.
DR BioMuta; CRMP1; -.
DR DMDM; 3122031; -.
DR EPD; Q14194; -.
DR jPOST; Q14194; -.
DR MassIVE; Q14194; -.
DR MaxQB; Q14194; -.
DR PaxDb; Q14194; -.
DR PeptideAtlas; Q14194; -.
DR PRIDE; Q14194; -.
DR ProteomicsDB; 59915; -. [Q14194-1]
DR ProteomicsDB; 59916; -. [Q14194-2]
DR ABCD; Q14194; 1 sequenced antibody.
DR Antibodypedia; 9351; 430 antibodies from 36 providers.
DR DNASU; 1400; -.
DR Ensembl; ENST00000324989.12; ENSP00000321606.7; ENSG00000072832.15. [Q14194-2]
DR Ensembl; ENST00000397890.6; ENSP00000380987.2; ENSG00000072832.15. [Q14194-1]
DR GeneID; 1400; -.
DR KEGG; hsa:1400; -.
DR MANE-Select; ENST00000324989.12; ENSP00000321606.7; NM_001014809.3; NP_001014809.1. [Q14194-2]
DR UCSC; uc003giq.5; human. [Q14194-1]
DR CTD; 1400; -.
DR DisGeNET; 1400; -.
DR GeneCards; CRMP1; -.
DR HGNC; HGNC:2365; CRMP1.
DR HPA; ENSG00000072832; Tissue enhanced (brain, pituitary gland, retina).
DR MIM; 602462; gene.
DR neXtProt; NX_Q14194; -.
DR OpenTargets; ENSG00000072832; -.
DR PharmGKB; PA26885; -.
DR VEuPathDB; HostDB:ENSG00000072832; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR InParanoid; Q14194; -.
DR OMA; IKYPMGK; -.
DR PhylomeDB; Q14194; -.
DR TreeFam; TF314706; -.
DR PathwayCommons; Q14194; -.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR SignaLink; Q14194; -.
DR SIGNOR; Q14194; -.
DR BioGRID-ORCS; 1400; 14 hits in 1060 CRISPR screens.
DR ChiTaRS; CRMP1; human.
DR GeneWiki; CRMP1; -.
DR GenomeRNAi; 1400; -.
DR Pharos; Q14194; Tbio.
DR PRO; PR:Q14194; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14194; protein.
DR Bgee; ENSG00000072832; Expressed in cortical plate and 145 other tissues.
DR ExpressionAtlas; Q14194; baseline and differential.
DR Genevisible; Q14194; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:HGNC.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0031005; F:filamin binding; IPI:WormBase.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:1904530; P:negative regulation of actin filament binding; IDA:WormBase.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:WormBase.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR CDD; cd01314; D-HYD; 1.
DR DisProt; DP02620; -.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030624; CRMP1.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF54; PTHR11647:SF54; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nitration; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 1"
FT /id="PRO_0000165909"
FT REGION 513..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 246..247
FT /note="Required for interaction with FLNA"
FT /evidence="ECO:0000269|PubMed:25358863"
FT COMPBIAS 515..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62950"
FT MOD_RES 101
FT /note="Phosphothreonine; by AURKA"
FT /evidence="ECO:0000269|PubMed:19799413"
FT MOD_RES 102
FT /note="Phosphothreonine; by AURKA"
FT /evidence="ECO:0000269|PubMed:19799413"
FT MOD_RES 316
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 504
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62950"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:25358863"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT VAR_SEQ 1..13
FT /note="MSYQGKKSIPHIT -> MADRRRAWNTEDDLPVYLARPGSAAQTPRQKYGGM
FT FAAVEGAYENKTIDFDAYSVGRRGSARTPRSAGRPDAVGLPGPGGSEDTASDVSEPSGS
FT AVSSPGERDERPPTLRIRRPAPRDLPLGRDNGQ (in isoform LCRMP-1)"
FT /evidence="ECO:0000303|PubMed:19362386"
FT /id="VSP_042545"
FT VARIANT 461
FT /note="V -> I (in dbSNP:rs34611001)"
FT /id="VAR_037745"
FT MUTAGEN 101..102
FT /note="TT->AA: 2.5-fold increase in cells with a defect of
FT cytokinesis."
FT /evidence="ECO:0000269|PubMed:19799413"
FT CONFLICT 351..370
FT /note="Missing (in Ref. 7; AAK55500)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="Y -> H (in Ref. 8; AAA93201)"
FT /evidence="ECO:0000305"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:4B3Z"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:4B3Z"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4B3Z"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:4B3Z"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:4B3Z"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:4B3Z"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:4B3Z"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:4B3Z"
FT HELIX 476..489
FT /evidence="ECO:0007829|PDB:4B3Z"
SQ SEQUENCE 572 AA; 62184 MW; A5385FCC79328A30 CRC64;
MSYQGKKSIP HITSDRLLIK GGRIINDDQS LYADVYLEDG LIKQIGENLI VPGGVKTIEA
NGRMVIPGGI DVNTYLQKPS QGMTAADDFF QGTRAALVGG TTMIIDHVVP EPGSSLLTSF
EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDVYQMSDSQ
LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI
TIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE
RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKLKTI
TAKSHKSAVE YNIFEGMECH GSPLVVISQG KIVFEDGNIN VNKGMGRFIP RKAFPEHLYQ
RVKIRNKVFG LQGVSRGMYD GPVYEVPATP KYATPAPSAK SSPSKHQPPP IRNLHQSNFS
LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG
