ARHGG_HUMAN
ID ARHGG_HUMAN Reviewed; 709 AA.
AC Q5VV41; Q86TF0; Q99434;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Rho guanine nucleotide exchange factor 16;
DE AltName: Full=Ephexin-4;
GN Name=ARHGEF16; Synonyms=EPHEXIN4, NBR;
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 2), AND VARIANT TYR-370.
RA Sasaki S., Takei Y., Ito M., Nakagawara A., Fujiwara T., Takahashi E.,
RA Muto T., Tokino T., Nakamura Y.;
RT "Isolation and characterization of a candidate gene for human neuroblastoma
RT mapped to 1p36.3, NBR: a new member of the Rho/Rac GEF family.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TYR-370.
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 156-709, AND VARIANT TYR-370.
RC TISSUE=PNS;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-107; SER-208;
RP SER-227; SER-230 AND SER-240, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, AND INTERACTION WITH ELMO2; EPHA2; RAC1 AND RHOG.
RX PubMed=20679435; DOI=10.1083/jcb.201005141;
RA Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
RA Negishi M., Katoh H.;
RT "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
RT mechanism.";
RL J. Cell Biol. 190:461-477(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-107; SER-174 AND
RP SER-191, AND IDENTIFICATION BY 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 [10]
RP INTERACTION WITH CDC42 AND TAX1BP3, AND INDUCTION BY HPV16 E6.
RX PubMed=21139582; DOI=10.1038/sj.bjc.6606026;
RA Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.;
RT "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which
RT activates Cdc42.";
RL Br. J. Cancer 104:324-331(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-107; SER-208 AND SER-230, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-174; SER-191 AND
RP SER-208, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [13]
RP STRUCTURE BY NMR OF 622-687.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the SH3 domain of human rho guanine exchange factor
RT (GEF) 16.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP VARIANT TRP-24.
RX PubMed=30245514; DOI=10.1038/s41436-018-0285-0;
RA Booth K.T., Askew J.W., Talebizadeh Z., Huygen P.L.M., Eudy J., Kenyon J.,
RA Hoover D., Hildebrand M.S., Smith K.R., Bahlo M., Kimberling W.J.,
RA Smith R.J.H., Azaiez H., Smith S.D.;
RT "Splice-altering variant in COL11A1 as a cause of nonsyndromic hearing loss
RT DFNA37.";
RL Genet. Med. 21:948-954(2019).
CC -!- FUNCTION: Guanyl-nucleotide exchange factor of the RHOG GTPase
CC stimulating the exchange of RHOG-associated GDP for GTP. May play a
CC role in chemotactic cell migration by mediating the activation of RAC1
CC by EPHA2. May also activate CDC42 and mediate activation of CDC42 by
CC the viral protein HPV16 E6. {ECO:0000269|PubMed:20679435}.
CC -!- SUBUNIT: Interacts with ELMO2, EPHA2, RAC1 and RHOG; mediates
CC activation of RAC1 by EPHA2. Interacts with TAX1BP3 (via PDZ domain).
CC May interact with CDC42; stimulated by HPV16 E6.
CC {ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:21139582}.
CC -!- INTERACTION:
CC Q5VV41; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-1057448, EBI-11983447;
CC Q5VV41; Q12959: DLG1; NbExp=3; IntAct=EBI-1057448, EBI-357481;
CC Q5VV41; P31943: HNRNPH1; NbExp=3; IntAct=EBI-1057448, EBI-351590;
CC Q5VV41; Q14847-2: LASP1; NbExp=3; IntAct=EBI-1057448, EBI-9088686;
CC Q5VV41; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-1057448, EBI-716006;
CC Q5VV41; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-1057448, EBI-741424;
CC Q5VV41; Q14160: SCRIB; NbExp=2; IntAct=EBI-1057448, EBI-357345;
CC Q5VV41; Q05BK6: TFG; NbExp=3; IntAct=EBI-1057448, EBI-10246902;
CC Q5VV41; Q92734: TFG; NbExp=3; IntAct=EBI-1057448, EBI-357061;
CC Q5VV41; P63104: YWHAZ; NbExp=2; IntAct=EBI-1057448, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VV41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VV41-2; Sequence=VSP_018149;
CC -!- INDUCTION: Up-regulated by HPV16 E6 (at protein level).
CC {ECO:0000269|PubMed:21139582}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with TAX1BP3.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02681.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D89016; BAA13745.1; -; mRNA.
DR EMBL; BT007270; AAP35934.1; -; mRNA.
DR EMBL; AL512413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002681; AAH02681.1; ALT_INIT; mRNA.
DR EMBL; BC051838; AAH51838.1; -; mRNA.
DR CCDS; CCDS46.2; -. [Q5VV41-1]
DR RefSeq; NP_055263.2; NM_014448.3. [Q5VV41-1]
DR RefSeq; XP_016856539.1; XM_017001050.1. [Q5VV41-1]
DR RefSeq; XP_016856540.1; XM_017001051.1. [Q5VV41-1]
DR PDB; 1X6B; NMR; -; A=622-687.
DR PDBsum; 1X6B; -.
DR AlphaFoldDB; Q5VV41; -.
DR BMRB; Q5VV41; -.
DR SMR; Q5VV41; -.
DR BioGRID; 118085; 80.
DR IntAct; Q5VV41; 40.
DR MINT; Q5VV41; -.
DR STRING; 9606.ENSP00000367629; -.
DR GlyGen; Q5VV41; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VV41; -.
DR PhosphoSitePlus; Q5VV41; -.
DR BioMuta; ARHGEF16; -.
DR DMDM; 74747198; -.
DR EPD; Q5VV41; -.
DR jPOST; Q5VV41; -.
DR MassIVE; Q5VV41; -.
DR MaxQB; Q5VV41; -.
DR PaxDb; Q5VV41; -.
DR PeptideAtlas; Q5VV41; -.
DR PRIDE; Q5VV41; -.
DR ProteomicsDB; 65436; -. [Q5VV41-1]
DR ProteomicsDB; 65437; -. [Q5VV41-2]
DR ABCD; Q5VV41; 7 sequenced antibodies.
DR Antibodypedia; 1622; 129 antibodies from 26 providers.
DR DNASU; 27237; -.
DR Ensembl; ENST00000378371.6; ENSP00000367622.2; ENSG00000130762.15. [Q5VV41-2]
DR Ensembl; ENST00000378373.5; ENSP00000367624.1; ENSG00000130762.15. [Q5VV41-2]
DR Ensembl; ENST00000378378.9; ENSP00000367629.4; ENSG00000130762.15. [Q5VV41-1]
DR GeneID; 27237; -.
DR KEGG; hsa:27237; -.
DR MANE-Select; ENST00000378378.9; ENSP00000367629.4; NM_014448.4; NP_055263.2.
DR UCSC; uc001akg.5; human. [Q5VV41-1]
DR CTD; 27237; -.
DR DisGeNET; 27237; -.
DR GeneCards; ARHGEF16; -.
DR HGNC; HGNC:15515; ARHGEF16.
DR HPA; ENSG00000130762; Tissue enhanced (intestine).
DR MIM; 618871; gene.
DR neXtProt; NX_Q5VV41; -.
DR OpenTargets; ENSG00000130762; -.
DR PharmGKB; PA24971; -.
DR VEuPathDB; HostDB:ENSG00000130762; -.
DR eggNOG; KOG3523; Eukaryota.
DR GeneTree; ENSGT01030000234571; -.
DR HOGENOM; CLU_012820_2_1_1; -.
DR InParanoid; Q5VV41; -.
DR OMA; FHPYVVY; -.
DR OrthoDB; 1176939at2759; -.
DR PhylomeDB; Q5VV41; -.
DR TreeFam; TF316357; -.
DR PathwayCommons; Q5VV41; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q5VV41; -.
DR BioGRID-ORCS; 27237; 11 hits in 1068 CRISPR screens.
DR ChiTaRS; ARHGEF16; human.
DR EvolutionaryTrace; Q5VV41; -.
DR GenomeRNAi; 27237; -.
DR Pharos; Q5VV41; Tbio.
DR PRO; PR:Q5VV41; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VV41; protein.
DR Bgee; ENSG00000130762; Expressed in mucosa of transverse colon and 143 other tissues.
DR ExpressionAtlas; Q5VV41; baseline and differential.
DR Genevisible; Q5VV41; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:BHF-UCL.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11938; SH3_ARHGEF16_26; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035797; ARHGEF16/ARHGEF26_SH3.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..709
FT /note="Rho guanine nucleotide exchange factor 16"
FT /id="PRO_0000233690"
FT DOMAIN 284..468
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 501..620
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 629..689
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 22..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..481
FT /note="Required for RHOG activation and mediates
FT interaction with EPHA2"
FT /evidence="ECO:0000269|PubMed:20679435"
FT MOTIF 707..709
FT /note="PDZ-binding motif"
FT COMPBIAS 53..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3U5C8"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_018149"
FT VARIANT 24
FT /note="R -> W (in dbSNP:rs562018000)"
FT /evidence="ECO:0000269|PubMed:30245514"
FT /id="VAR_083184"
FT VARIANT 137
FT /note="V -> M (in dbSNP:rs3806164)"
FT /id="VAR_059796"
FT VARIANT 370
FT /note="H -> Y (in dbSNP:rs2185639)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.2"
FT /id="VAR_059797"
FT VARIANT 681
FT /note="E -> K (in dbSNP:rs56309807)"
FT /id="VAR_061796"
FT CONFLICT 157..158
FT /note="AM -> RG (in Ref. 4; AAH02681)"
FT /evidence="ECO:0000305"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:1X6B"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:1X6B"
FT STRAND 654..662
FT /evidence="ECO:0007829|PDB:1X6B"
FT STRAND 665..670
FT /evidence="ECO:0007829|PDB:1X6B"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:1X6B"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:1X6B"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:1X6B"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1X6B"
SQ SEQUENCE 709 AA; 80105 MW; 9672AB3C92311BEB CRC64;
MAQRHSDSSL EEKLLGHRFH SELRLDAGGN PASGLPMVRG SPRVRDDAAF QPQVPAPPQP
RPPGHEEPWP IVLSTESPAA LKLGTQQLIP KSLAVASKAK TPARHQSFGA AVLSREAARR
DPKLLPAPSF SLDDMDVDKD PGGMLRRNLR NQSYRAAMKG LGKPGGQGDA IQLSPKLQAL
AEEPSQPHTR SPAKNKKTLG RKRGHKGSFK DDPQLYQEIQ ERGLNTSQES DDDILDESSS
PEGTQKVDAT IVVKSYRPAQ VTWSQLPEVV ELGILDQLST EERKRQEAMF EILTSEFSYQ
HSLSILVEEF LQSKELRATV TQMEHHHLFS NILDVLGASQ RFFEDLEQRH KAQVLVEDIS
DILEEHAEKH FHPYIAYCSN EVYQQRTLQK LISSNAAFRE ALREIERRPA CGGLPMLSFL
ILPMQRVTRL PLLMDTLCLK TQGHSERYKA ASRALKAISK LVRQCNEGAH RMERMEQMYT
LHTQLDFSKV KSLPLISASR WLLKRGELFL VEETGLFRKI ASRPTCYLFL FNDVLVVTKK
KSEESYMVQD YAQMNHIQVE KIEPSELPLP GGGNRSSSVP HPFQVTLLRN SEGRQEQLLL
SSDSASDRAR WIVALTHSER QWQGLSSKGD LPQVEITKAF FAKQADEVTL QQADVVLVLQ
QEDGWLYGER LRDGETGWFP EDFARFITSR VAVEGNVRRM ERLRVETDV
