PKHG3_HUMAN
ID PKHG3_HUMAN Reviewed; 1219 AA.
AC A1L390; A1L389; B5MEC9; O60339; Q6GMS3; Q6P4B1; Q7L3S3; Q86SW7; Q8TEF5;
AC Q96EW6; Q9BT82;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pleckstrin homology domain-containing family G member 3;
DE Short=PH domain-containing family G member 3 {ECO:0000305};
GN Name=PLEKHG3 {ECO:0000312|HGNC:HGNC:20364}; Synonyms=KIAA0599;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TRP-1036.
RC TISSUE=Brain, Lung, Pancreas, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-659 (ISOFORM 3).
RC TISSUE=Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-1219 (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-1219.
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-576; SER-577;
RP SER-643; SER-647; SER-741; SER-962; SER-1037 AND SER-1040, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-576; SER-577;
RP SER-1037 AND SER-1040, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-576; SER-577;
RP SER-631; SER-640; SER-643; SER-647; SER-741; SER-827; SER-1037 AND
RP SER-1040, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-631; SER-640;
RP SER-643; SER-647; SER-741; SER-827; SER-1037; SER-1040 AND SER-1081, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741 AND SER-1011, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=27555588; DOI=10.1073/pnas.1604720113;
RA Nguyen T.T., Park W.S., Park B.O., Kim C.Y., Oh Y., Kim J.M., Choi H.,
RA Kyung T., Kim C.H., Lee G., Hahn K.M., Meyer T., Heo W.D.;
RT "PLEKHG3 enhances polarized cell migration by activating actin filaments at
RT the cell front.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10091-10096(2016).
CC -!- FUNCTION: Plays a role in controlling cell polarity and cell motility
CC by selectively binding newly polymerized actin and activating RAC1 and
CC CDC42 to enhance local actin polymerization.
CC {ECO:0000269|PubMed:27555588}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:27555588}. Note=Colocalizes with actin at the
CC leading edge of polarized cells. {ECO:0000269|PubMed:27555588}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A1L390-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1L390-2; Sequence=VSP_028533, VSP_041513;
CC Name=3;
CC IsoId=A1L390-3; Sequence=VSP_028534;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84995.1; Type=Miscellaneous discrepancy; Note=Intron retention. There are two regions of intron retention within the sequence which cause it to shift frame.; Evidence={ECO:0000305};
CC Sequence=CAD66586.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL121774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004298; AAH04298.1; -; mRNA.
DR EMBL; BC011891; AAH11891.2; -; mRNA.
DR EMBL; BC063554; AAH63554.1; -; mRNA.
DR EMBL; BC073907; AAH73907.1; -; mRNA.
DR EMBL; BC129952; AAI29953.1; -; mRNA.
DR EMBL; BC129953; AAI29954.1; -; mRNA.
DR EMBL; BX248779; CAD66586.1; ALT_INIT; mRNA.
DR EMBL; AK074169; BAB84995.1; ALT_SEQ; mRNA.
DR EMBL; AB011171; BAA25525.1; -; mRNA.
DR CCDS; CCDS76690.1; -. [A1L390-1]
DR PIR; T00267; T00267.
DR RefSeq; NP_001295076.1; NM_001308147.1. [A1L390-1]
DR RefSeq; XP_016876646.1; XM_017021157.1. [A1L390-1]
DR AlphaFoldDB; A1L390; -.
DR SMR; A1L390; -.
DR BioGRID; 117496; 102.
DR IntAct; A1L390; 41.
DR MINT; A1L390; -.
DR STRING; 9606.ENSP00000247226; -.
DR iPTMnet; A1L390; -.
DR PhosphoSitePlus; A1L390; -.
DR BioMuta; PLEKHG3; -.
DR EPD; A1L390; -.
DR jPOST; A1L390; -.
DR MassIVE; A1L390; -.
DR MaxQB; A1L390; -.
DR PeptideAtlas; A1L390; -.
DR PRIDE; A1L390; -.
DR ProteomicsDB; 140; -. [A1L390-1]
DR ProteomicsDB; 141; -. [A1L390-2]
DR ProteomicsDB; 142; -. [A1L390-3]
DR Antibodypedia; 57155; 79 antibodies from 11 providers.
DR DNASU; 26030; -.
DR Ensembl; ENST00000247226.13; ENSP00000247226.8; ENSG00000126822.18. [A1L390-1]
DR Ensembl; ENST00000394691.7; ENSP00000378183.2; ENSG00000126822.18. [A1L390-3]
DR GeneID; 26030; -.
DR KEGG; hsa:26030; -.
DR MANE-Select; ENST00000247226.13; ENSP00000247226.8; NM_001308147.2; NP_001295076.1.
DR UCSC; uc001xhn.2; human. [A1L390-1]
DR CTD; 26030; -.
DR DisGeNET; 26030; -.
DR GeneCards; PLEKHG3; -.
DR HGNC; HGNC:20364; PLEKHG3.
DR HPA; ENSG00000126822; Tissue enhanced (brain).
DR MIM; 617940; gene.
DR neXtProt; NX_A1L390; -.
DR OpenTargets; ENSG00000126822; -.
DR PharmGKB; PA134925358; -.
DR VEuPathDB; HostDB:ENSG00000126822; -.
DR eggNOG; KOG3518; Eukaryota.
DR GeneTree; ENSGT00940000156521; -.
DR HOGENOM; CLU_007600_0_0_1; -.
DR InParanoid; A1L390; -.
DR OMA; IMQLSHV; -.
DR OrthoDB; 147068at2759; -.
DR PhylomeDB; A1L390; -.
DR TreeFam; TF328565; -.
DR PathwayCommons; A1L390; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; A1L390; -.
DR SIGNOR; A1L390; -.
DR BioGRID-ORCS; 26030; 123 hits in 1068 CRISPR screens.
DR GenomeRNAi; 26030; -.
DR Pharos; A1L390; Tbio.
DR PRO; PR:A1L390; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A1L390; protein.
DR Bgee; ENSG00000126822; Expressed in sural nerve and 169 other tissues.
DR ExpressionAtlas; A1L390; baseline and differential.
DR Genevisible; A1L390; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd13243; PH_PLEKHG1_G2_G3; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043324; PH_PLEKHG1_G2_G3.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1219
FT /note="Pleckstrin homology domain-containing family G
FT member 3"
FT /id="PRO_0000306863"
FT DOMAIN 93..272
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 296..394
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VAC9"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VAC9"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VAC9"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VAC9"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..466
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028533"
FT VAR_SEQ 118..173
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_028534"
FT VAR_SEQ 467..468
FT /note="MK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041513"
FT VARIANT 1014
FT /note="R -> H (in dbSNP:rs41309246)"
FT /id="VAR_061518"
FT VARIANT 1036
FT /note="R -> W (in dbSNP:rs229649)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035330"
FT CONFLICT 443..468
FT /note="QGRRQSEPTKHLLRQLNEKARAAGMK -> KGAGPEPPGSEEEEEEQEESLA
FT VAEQ (in Ref. 2; AAH04298)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..468
FT /note="KARAAGMK -> ESLAVAEQ (in Ref. 2; AAH73907)"
FT /evidence="ECO:0000305"
FT CONFLICT 723..736
FT /note="YYENAEHHDAGFSV -> WWPHCTPASCSSPT (in Ref. 2;
FT AAH04298)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="R -> S (in Ref. 2; AAI29953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1219 AA; 134412 MW; DAEB5673340F4FBD CRC64;
MPVSTSLHQD GSQERPVSLT STTSSSGSSC DSRSAMEEPS SSEAPAKNGA GSLRSRHLPN
SNNNSSSWLN VKGPLSPFNS RAAAGPAHHK LSYLGRVVRE IVETERMYVQ DLRSIVEDYL
LKIIDTPGLL KPEQVSALFG NIENIYALNS QLLRDLDSCN SDPVAVASCF VERSQEFDIY
TQYCNNYPNS VAALTECMRD KQQAKFFRDR QELLQHSLPL GSYLLKPVQR ILKYHLLLQE
IAKHFDEEED GFEVVEDAID TMTCVAWYIN DMKRRHEHAV RLQEIQSLLI NWKGPDLTTY
GELVLEGTFR VHRVRNERTF FLFDKTLLIT KKRGDHFVYK GNIPCSSLML IESTRDSLCF
TVTHYKHSKQ QYSIQAKTVE EKRNWTHHIK RLILENHHAT IPQKAKEAIL EMDSYYPNRY
RCSPERLKKA WSSQDEVSTN VRQGRRQSEP TKHLLRQLNE KARAAGMKGK GRRESESSRS
SRRPSGRSPT STEKRMSFES ISSLPEVEPD PEAGSEQEVF SAVEGPSAEE TPSDTESPEV
LETQLDAHQG LLGMDPPGDM VDFVAAESTE DLKALSSEEE EEMGGAAQEP ESLLPPSVLD
QASVIAERFV SSFSRRSSVA QEDSKSSGFG SPRLVSRSSS VLSLEGSEKG LARHGSATDS
LSCQLSPEVD ISVGVATEDS PSVNGMEPPS PGCPVEPDRS SCKKKESALS TRDRLLLDKI
KSYYENAEHH DAGFSVRRRE SLSYIPKGLV RNSISRFNSL PRPDPEPVPP VGSKRQVGSR
PTSWALFELP GPSQAVKGDP PPISDAEFRP SSEIVKIWEG MESSGGSPGK GPGQGQANGF
DLHEPLFILE EHELGAITEE SATASPESSS PTEGRSPAHL ARELKELVKE LSSSTQGELV
APLHPRIVQL SHVMDSHVSE RVKNKVYQLA RQYSLRIKSN KPVMARPPLQ WEKVAPERDG
KSPTVPCLQE EAGEPLGGKG KRKPVLSLFD YEQLMAQEHS PPKPSSAGEM SPQRFFFNPS
AVSQRTTSPG GRPSARSPLS PTETFSWPDV RELCSKYASR DEARRAGGGR PRGPPVNRSH
SVPENMVEPP LSGRVGRCRS LSTKRGRGGG EAAQSPGPLP QSKPDGGETL YVTADLTLED
NRRVIVMEKG PLPSPTAGLE ESSGQGPSSP VALLGQVQDF QQSAECQPKE EGSRDPADPS
QQGRVRNLRE KFQALNSVG
