CDC42_RAT
ID CDC42_RAT Reviewed; 191 AA.
AC Q8CFN2; Q6P9Y3; Q71TW5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cell division control protein 42 homolog {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:25498153};
DE Flags: Precursor;
GN Name=Cdc42 {ECO:0000312|RGD:71043};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11048641; DOI=10.1038/emm.2000.20;
RA Han J.-S., Kim J.-H., Kim J.G., Park J.-B., Noh D.-Y., Lee K.-H.;
RT "Molecular cloning and sequencing of rat Cdc42 GTPase cDNA.";
RL Exp. Mol. Med. 32:115-119(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RA Chen D., Manabu M., Lan J., Jin J., Simon R.P.;
RT "The cdc42 plays a protective role in the brain ischemia.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
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 [4]
RP PROTEIN SEQUENCE OF 6-16; 108-120 AND 167-183, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21423166; DOI=10.1038/nature09823;
RA Murakoshi H., Wang H., Yasuda R.;
RT "Local, persistent activation of Rho GTPases during plasticity of single
RT dendritic spines.";
RL Nature 472:100-104(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=25498153; DOI=10.7554/elife.03116;
RA Galic M., Tsai F.C., Collins S.R., Matis M., Bandara S., Meyer T.;
RT "Dynamic recruitment of the curvature-sensitive protein ArhGAP44 to
RT nanoscale membrane deformations limits exploratory filopodia initiation in
RT neurons.";
RL Elife 3:E03116-E03116(2014).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and an inactive GDP-bound state. In active state
CC binds to a variety of effector proteins to regulate cellular responses
CC (PubMed:25498153). Involved in epithelial cell polarization processes.
CC Regulates the bipolar attachment of spindle microtubules to
CC kinetochores before chromosome congression in metaphase (By
CC similarity). Regulates cell migration (By similarity). In neurons,
CC plays a role in the extension and maintenance of the formation of
CC filopodia, thin and actin-rich surface projections (By similarity).
CC Required for DOCK10-mediated spine formation in Purkinje cells and
CC hippocampal neurons. Facilitates filopodia formation upon DOCK11-
CC activation (By similarity). Upon activation by CaMKII, modulates
CC dendritic spine structural plasticity by relaying CaMKII transient
CC activation to synapse-specific, long-term signaling (PubMed:21423166,
CC PubMed:25498153). Also plays a role in phagocytosis through
CC organization of the F-actin cytoskeleton associated with forming
CC phagocytic cups (By similarity). {ECO:0000250|UniProtKB:P60766,
CC ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:21423166,
CC ECO:0000269|PubMed:25498153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:25498153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:25498153};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase (Probable). Inhibited by GAPs such as
CC ARHGAP44 (PubMed:25498153). {ECO:0000269|PubMed:25498153, ECO:0000305}.
CC -!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4,
CC CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-
CC dependent manner). Interacts with activated CSPG4 and with BAIAP2.
CC Interacts with DOCK11/Zizimin2; the interaction activates CDC42 by
CC exchanging GDP for GTP. Interacts with DOCK9; the interaction activates
CC CDC42 by exchanging GDP for GTP. Interacts with DOCK8 (via DHR-2
CC domain); the interaction activates CDC42 by exchanging GDP for GTP.
CC Interacts with IQGAP1. Interacts with NET1 and ARHGAP33/TCGAP. Part of
CC a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. The GTP-
CC bound form interacts with CCPG1. Interacts with USP6. Interacts with
CC NEK6. Part of a collagen stimulated complex involved in cell migration
CC composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with
CC ITGB1BP1. Interacts with ARHGDIA; this interaction inactivates and
CC stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the
CC inactive, GDP-bound form. Interacts in (GTP-bound form) with FNBP1L and
CC ABI1, but only in the presence of FNBP1L.
CC {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953}.
CC -!- INTERACTION:
CC Q8CFN2; Q9UQB8: BAIAP2; Xeno; NbExp=2; IntAct=EBI-7023929, EBI-525456;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P60766};
CC Lipid-anchor {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P60766}. Midbody {ECO:0000250|UniProtKB:P60953}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P60953}. Cytoplasm
CC {ECO:0000250|UniProtKB:P60766}. Cell projection, lamellipodium membrane
CC {ECO:0000250|UniProtKB:P60766}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P60766}. Cell projection, dendrite
CC {ECO:0000305|PubMed:21423166}. Note=Localizes to spindle during
CC prometaphase cells. Moves to the central spindle as cells progressed
CC through anaphase to telophase. Localizes at the end of cytokinesis in
CC the intercellular bridge formed between two daughter cells. Its
CC localization is regulated by the activities of guanine nucleotide
CC exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes
CC with NEK6 in the centrosome. In its active GTP-bound form localizes to
CC the leading edge membrane of migrating dendritic cells.
CC {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CFN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CFN2-2; Sequence=VSP_022241;
CC -!- PTM: Phosphorylated by SRC in an EGF-dependent manner, this stimulates
CC the binding of the Rho-GDP dissociation inhibitor RhoGDI.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000305}.
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DR EMBL; AF205635; AAF15538.1; -; mRNA.
DR EMBL; AF491841; AAN63806.1; -; mRNA.
DR EMBL; BC060535; AAH60535.1; -; mRNA.
DR RefSeq; NP_741991.3; NM_171994.4. [Q8CFN2-1]
DR RefSeq; XP_008762508.1; XM_008764286.2. [Q8CFN2-1]
DR RefSeq; XP_008762509.1; XM_008764287.2.
DR AlphaFoldDB; Q8CFN2; -.
DR SMR; Q8CFN2; -.
DR BioGRID; 249080; 4.
DR CORUM; Q8CFN2; -.
DR ELM; Q8CFN2; -.
DR IntAct; Q8CFN2; 5.
DR MINT; Q8CFN2; -.
DR STRING; 10116.ENSRNOP00000030928; -.
DR ChEMBL; CHEMBL3308943; -.
DR iPTMnet; Q8CFN2; -.
DR PhosphoSitePlus; Q8CFN2; -.
DR SwissPalm; Q8CFN2; -.
DR jPOST; Q8CFN2; -.
DR PaxDb; Q8CFN2; -.
DR PRIDE; Q8CFN2; -.
DR Ensembl; ENSRNOT00000029025; ENSRNOP00000030928; ENSRNOG00000013536. [Q8CFN2-1]
DR GeneID; 64465; -.
DR KEGG; rno:64465; -.
DR UCSC; RGD:71043; rat. [Q8CFN2-1]
DR CTD; 998; -.
DR RGD; 71043; Cdc42.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153675; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q8CFN2; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q8CFN2; -.
DR TreeFam; TF101109; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-182971; EGFR downregulation.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-525793; Myogenesis.
DR Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
DR Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q8CFN2; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013536; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q8CFN2; baseline and differential.
DR Genevisible; Q8CFN2; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:BHF-UCL.
DR GO; GO:0017119; C:Golgi transport complex; ISO:RGD.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031256; C:leading edge membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000322; C:storage vacuole; ISO:RGD.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; ISO:RGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0032427; F:GBD domain binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0031996; F:thioesterase binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0090135; P:actin filament branching; IMP:RGD.
DR GO; GO:0007015; P:actin filament organization; IMP:RGD.
DR GO; GO:0034332; P:adherens junction organization; ISO:RGD.
DR GO; GO:0003161; P:cardiac conduction system development; ISO:RGD.
DR GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; ISO:RGD.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IDA:SynGO.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0036336; P:dendritic cell migration; ISO:RGD.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0086101; P:endothelin receptor signaling pathway involved in heart process; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; TAS:RGD.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:BHF-UCL.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0046847; P:filopodium assembly; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; IMP:BHF-UCL.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0099563; P:modification of synaptic structure; IMP:SynGO.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0048664; P:neuron fate determination; ISO:RGD.
DR GO; GO:0038189; P:neuropilin signaling pathway; ISO:RGD.
DR GO; GO:0007097; P:nuclear migration; ISO:RGD.
DR GO; GO:0051647; P:nucleus localization; ISO:RGD.
DR GO; GO:0072384; P:organelle transport along microtubule; IMP:BHF-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISS:UniProtKB.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; IMP:RGD.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; TAS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; ISO:RGD.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; IMP:SynGO.
DR GO; GO:0043393; P:regulation of protein binding; ISO:RGD.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; TAS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:RGD.
DR GO; GO:0060661; P:submandibular salivary gland formation; IEP:RGD.
DR GO; GO:0039694; P:viral RNA genome replication; ISO:RGD.
DR CDD; cd01874; Cdc42; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037874; Cdc42.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Differentiation; Direct protein sequencing; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Cell division control protein 42 homolog"
FT /id="PRO_0000270829"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000270830"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P60953"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 182..191
FT /note="PKKSRRCVLL -> TQPKRKCCIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11048641"
FT /id="VSP_022241"
FT CONFLICT 159
FT /note="A -> P (in Ref. 1; AAF15538 and 2; AAN63806)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="K -> R (in Ref. 1; AAF15538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21259 MW; 51A437E22A4D8FFF CRC64;
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
EPKKSRRCVL L
