RHG29_HUMAN
ID RHG29_HUMAN Reviewed; 1261 AA.
AC Q52LW3; O15463; Q59H86; Q5VYZ0; Q6NVX2; Q8TBI6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rho GTPase-activating protein 29;
DE AltName: Full=PTPL1-associated RhoGAP protein 1;
DE AltName: Full=Rho-type GTPase-activating protein 29;
GN Name=ARHGAP29; Synonyms=PARG1;
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), PROTEIN SEQUENCE OF 64-72; 221-228;
RP 349-357; 456-468; 666-678; 943-946; 971-985; 1015-1024; 1069-1079 AND
RP 1212-1224, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PTPN13, AND
RP VARIANT ASP-1255.
RC TISSUE=Skeletal muscle;
RX PubMed=9305890; DOI=10.1074/jbc.272.39.24333;
RA Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J., Heldin C.-H.;
RT "A novel GTPase-activating protein for Rho interacts with a PDZ domain of
RT the protein-tyrosine phosphatase PTPL1.";
RL J. Biol. Chem. 272:24333-24338(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-1261 (ISOFORM 1), AND VARIANT
RP ASP-1255.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=11716068; DOI=10.1023/a:1012253317934;
RA Mariani L., Beaudry C., McDonough W.S., Hoelzinger D.B., Demuth T.,
RA Ross K.R., Berens T., Coons S.W., Watts G., Trent J.M., Wei J.S., Giese A.,
RA Berens M.E.;
RT "Glioma cell motility is associated with reduced transcription of
RT proapoptotic and proliferation genes: a cDNA microarray analysis.";
RL J. Neurooncol. 53:161-176(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH RAP2A.
RX PubMed=15752761; DOI=10.1016/j.bbrc.2005.02.069;
RA Myagmar B.-E., Umikawa M., Asato T., Taira K., Oshiro M., Hino A.,
RA Takei K., Uezato H., Kariya K.;
RT "PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative
RT Rap2 effector.";
RL Biochem. Biophys. Res. Commun. 329:1046-1052(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1019, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP INDUCTION.
RX PubMed=17488656; DOI=10.3324/haematol.10337;
RA Ripperger T., von Neuhoff N., Kamphues K., Emura M., Lehmann U.,
RA Tauscher M., Schraders M., Groenen P., Skawran B., Rudolph C.,
RA Callet-Bauchu E., van Krieken J.H., Schlegelberger B., Steinemann D.;
RT "Promoter methylation of PARG1, a novel candidate tumor suppressor gene in
RT mantle-cell lymphomas.";
RL Haematologica 92:460-468(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-179; SER-949 AND
RP SER-1146, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP 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 [13]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-552.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. Has strong activity toward RHOA, and
CC weaker activity toward RAC1 and CDC42. May act as a specific effector
CC of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA
CC signaling and dampens ROCK and MYH9 activities in endothelial cells and
CC plays an essential role in blood vessel tubulogenesis.
CC {ECO:0000269|PubMed:15752761, ECO:0000269|PubMed:9305890}.
CC -!- SUBUNIT: Interacts with PTPN13/PTPL1. Interacts with RAP2A via its
CC coiled coil domain. Interacts with RASIP1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q52LW3-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-22012297, EBI-10988864;
CC Q52LW3-2; P42858: HTT; NbExp=3; IntAct=EBI-22012297, EBI-466029;
CC Q52LW3-2; O14901: KLF11; NbExp=3; IntAct=EBI-22012297, EBI-948266;
CC Q52LW3-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-22012297, EBI-2811583;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q52LW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q52LW3-2; Sequence=VSP_031058, VSP_031059;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal
CC muscle and heart. Expressed at intermediate level in placenta, liver
CC and pancreas. Weakly expressed in brain, lung and kidney.
CC {ECO:0000269|PubMed:9305890}.
CC -!- INDUCTION: Strongly down-regulated in mantle-cell lymphomas. Up-
CC regulated in migrating glioma cells. {ECO:0000269|PubMed:11716068,
CC ECO:0000269|PubMed:17488656}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH67839.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; U90920; AAB81012.1; -; mRNA.
DR EMBL; AL162735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73052.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73051.1; -; Genomic_DNA.
DR EMBL; BC022483; AAH22483.1; -; mRNA.
DR EMBL; BC067839; AAH67839.1; ALT_SEQ; mRNA.
DR EMBL; BC093741; AAH93741.1; -; mRNA.
DR EMBL; BC093767; AAH93767.1; -; mRNA.
DR EMBL; AB208873; BAD92110.1; -; mRNA.
DR CCDS; CCDS748.1; -. [Q52LW3-1]
DR PIR; E59430; E59430.
DR RefSeq; NP_001315593.1; NM_001328664.1. [Q52LW3-1]
DR RefSeq; NP_004806.3; NM_004815.3. [Q52LW3-1]
DR RefSeq; XP_011540741.1; XM_011542439.2. [Q52LW3-1]
DR AlphaFoldDB; Q52LW3; -.
DR SMR; Q52LW3; -.
DR BioGRID; 114806; 62.
DR IntAct; Q52LW3; 30.
DR MINT; Q52LW3; -.
DR STRING; 9606.ENSP00000260526; -.
DR GlyGen; Q52LW3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q52LW3; -.
DR PhosphoSitePlus; Q52LW3; -.
DR BioMuta; ARHGAP29; -.
DR DMDM; 166977701; -.
DR EPD; Q52LW3; -.
DR jPOST; Q52LW3; -.
DR MassIVE; Q52LW3; -.
DR MaxQB; Q52LW3; -.
DR PaxDb; Q52LW3; -.
DR PeptideAtlas; Q52LW3; -.
DR PRIDE; Q52LW3; -.
DR ProteomicsDB; 62427; -. [Q52LW3-1]
DR ProteomicsDB; 62428; -. [Q52LW3-2]
DR Antibodypedia; 19948; 106 antibodies from 18 providers.
DR DNASU; 9411; -.
DR Ensembl; ENST00000260526.11; ENSP00000260526.6; ENSG00000137962.13. [Q52LW3-1]
DR Ensembl; ENST00000370217.3; ENSP00000359237.3; ENSG00000137962.13. [Q52LW3-2]
DR GeneID; 9411; -.
DR KEGG; hsa:9411; -.
DR MANE-Select; ENST00000260526.11; ENSP00000260526.6; NM_004815.4; NP_004806.3.
DR UCSC; uc001dqj.5; human. [Q52LW3-1]
DR CTD; 9411; -.
DR DisGeNET; 9411; -.
DR GeneCards; ARHGAP29; -.
DR HGNC; HGNC:30207; ARHGAP29.
DR HPA; ENSG00000137962; Low tissue specificity.
DR MalaCards; ARHGAP29; -.
DR MIM; 610496; gene.
DR neXtProt; NX_Q52LW3; -.
DR OpenTargets; ENSG00000137962; -.
DR Orphanet; 199306; Cleft lip/palate.
DR PharmGKB; PA128394548; -.
DR VEuPathDB; HostDB:ENSG00000137962; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_059009_0_0_1; -.
DR InParanoid; Q52LW3; -.
DR OMA; QMIFDTP; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q52LW3; -.
DR TreeFam; TF351450; -.
DR PathwayCommons; Q52LW3; -.
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 SignaLink; Q52LW3; -.
DR SIGNOR; Q52LW3; -.
DR BioGRID-ORCS; 9411; 65 hits in 1077 CRISPR screens.
DR ChiTaRS; ARHGAP29; human.
DR GenomeRNAi; 9411; -.
DR Pharos; Q52LW3; Tbio.
DR PRO; PR:Q52LW3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q52LW3; protein.
DR Bgee; ENSG00000137962; Expressed in visceral pleura and 200 other tissues.
DR ExpressionAtlas; Q52LW3; baseline and differential.
DR Genevisible; Q52LW3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW GTPase activation; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1261
FT /note="Rho GTPase-activating protein 29"
FT /id="PRO_0000317582"
FT DOMAIN 192..462
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 671..886
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 612..657
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 481..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1261
FT /note="Interaction with PTPN13/PTPL1"
FT /evidence="ECO:0000269|PubMed:9305890"
FT COILED 296..418
FT /evidence="ECO:0000255"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQJ5"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQJ5"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 383..393
FT /note="EEANELYKVCV -> TIFFFFICKLN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031058"
FT VAR_SEQ 394..1261
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031059"
FT VARIANT 552
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038552"
FT VARIANT 1192
FT /note="P -> L (in dbSNP:rs11165091)"
FT /id="VAR_049145"
FT VARIANT 1255
FT /note="G -> D (in dbSNP:rs1999272)"
FT /evidence="ECO:0000269|PubMed:9305890, ECO:0000269|Ref.5"
FT /id="VAR_038553"
FT CONFLICT 58
FT /note="M -> I (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="L -> F (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="S -> Y (in Ref. 4; AAH67839)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="A -> V (in Ref. 5; BAD92110)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="N -> D (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="L -> V (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="S -> R (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="D -> G (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="Q -> L (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="Q -> L (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="T -> Q (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="T -> A (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="V -> C (in Ref. 1; AAB81012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1261 AA; 142064 MW; 3E46445EA5DA76C8 CRC64;
MIAHKQKKTK KKRAWASGQL STDITTSEMG LKSLSSNSIF DPDYIKELVN DIRKFSHMLL
YLKEAIFSDC FKEVIHIRLE ELLRVLKSIM NKHQNLNSVD LQNAAEMLTA KVKAVNFTEV
NEENKNDLFQ EVFSSIETLA FTFGNILTNF LMGDVGNDSL LRLPVSRETK SFENVSVESV
DSSSEKGNFS PLELDNVLLK NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNM
VKLAEATRTN IGIQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM
EKQRKEIKEL WKQEQNKMLE AENALKKAKL LCMQRQDEYE KAKSSMFRAE EEHLSSSGGL
AKNLNKQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR NDLENTKREI LAQLRTLVFQ
CDLTLKAVTV NLFHMQHLQA ASLADSLQSL CDSAKLYDPG QEYSEFVKAT NSTEEEKVDG
NVNKHLNSSQ PSGFGPANSL EDVVRLPDSS NKIEEDRCSN SADITGPSFI RSWTFGMFSD
SESTGGSSES RSLDSESISP GDFHRKLPRT PSSGTMSSAD DLDEREPPSP SETGPNSLGT
FKKTLMSKAA LTHKFRKLRS PTKCRDCEGI VVFQGVECEE CLLVCHRKCL ENLVIICGHQ
KLPGKIHLFG AEFTQVAKKE PDGIPFILKI CASEIENRAL CLQGIYRVCG NKIKTEKLCQ
ALENGMHLVD ISEFSSHDIC DVLKLYLRQL PEPFILFRLY KEFIDLAKEI QHVNEEQETK
KNSLEDKKWP NMCIEINRIL LKSKDLLRQL PASNFNSLHF LIVHLKRVVD HAEENKMNSK
NLGVIFGPSL IRPRPTTAPI TISSLAEYSN QARLVEFLIT YSQKIFDGSL QPQDVMCSIG
VVDQGCFPKP LLSPEERDIE RSMKSLFFSS KEDIHTSESE SKIFERATSF EESERKQNAL
GKCDACLSDK AQLLLDQEAE SASQKIEDGK TPKPLSLKSD RSTNNVERHT PRTKIRPVSL
PVDRLLLASP PNERNGRNMG NVNLDKFCKN PAFEGVNRKD AATTVCSKFN GFDQQTLQKI
QDKQYEQNSL TAKTTMIMPS ALQEKGVTTS LQISGDHSIN ATQPSKPYAE PVRSVREASE
RRSSDSYPLA PVRAPRTLQP QHWTTFYKPH APIISIRGNE EKPASPSAAV PPGTDHDPHG
LVVKSMPDPD KASACPGQAT GQPKEDSEEL GLPDVNPMCQ RPRLKRMQQF EDLEGEIPQF
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