PREX1_HUMAN
ID PREX1_HUMAN Reviewed; 1659 AA.
AC Q8TCU6; E1P5X9; Q5JS95; Q5JS96; Q69YL2; Q7Z2L9; Q9BQH0; Q9BX55; Q9H4Q6;
AC Q9P2D2; Q9UGQ4;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein;
DE Short=P-Rex1;
DE Short=PtdIns(3,4,5)-dependent Rac exchanger 1;
GN Name=PREX1; Synonyms=KIAA1415;
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 182-198;
RP 913-920; 1463-1470; 1501-1506 AND 1590-1604, CHARACTERIZATION, AND VARIANTS
RP THR-1118 AND GLU-1340.
RX PubMed=11955434; DOI=10.1016/s0092-8674(02)00663-3;
RA Welch H.C.E., Coadwell W.J., Ellson C.D., Ferguson G.J., Andrews S.R.,
RA Erdjument-Bromage H., Tempst P., Hawkins P.T., Stephens L.R.;
RT "P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide
RT exchange factor for Rac.";
RL Cell 108:809-821(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-1340.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-1659 (ISOFORM 1), AND VARIANT
RP GLU-1340.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-1659 (ISOFORM 1), AND VARIANT
RP GLU-1340.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1659 (ISOFORM 1), AND
RP VARIANTS MET-659; HIS-786; ILE-1240 AND GLU-1340.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1200, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 607-706.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the first PDZ domain of PREX1.";
RL Submitted (FEB-2011) to the PDB data bank.
CC -!- FUNCTION: Functions as a RAC guanine nucleotide exchange factor (GEF),
CC which activates the Rac proteins by exchanging bound GDP for free GTP.
CC Its activity is synergistically activated by phosphatidylinositol
CC 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G
CC protein. May function downstream of heterotrimeric G proteins in
CC neutrophils.
CC -!- SUBUNIT: Interacts preferentially with RAC2. Interacts with RAC1.
CC Interacts with AUTS2. {ECO:0000250|UniProtKB:Q69ZK0}.
CC -!- INTERACTION:
CC Q8TCU6; P60953-2: CDC42; NbExp=2; IntAct=EBI-1046542, EBI-287394;
CC Q8TCU6; P42345: MTOR; NbExp=11; IntAct=EBI-1046542, EBI-359260;
CC Q8TCU6; P63000-1: RAC1; NbExp=2; IntAct=EBI-1046542, EBI-7212896;
CC Q8TCU6; Q6R327: RICTOR; NbExp=3; IntAct=EBI-1046542, EBI-1387196;
CC Q8TCU6; Q8N122: RPTOR; NbExp=2; IntAct=EBI-1046542, EBI-1567928;
CC Q8TCU6; P31750: Akt1; Xeno; NbExp=2; IntAct=EBI-1046542, EBI-298707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mainly
CC cytosolic. Some amount is apparently associated to the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TCU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCU6-2; Sequence=VSP_001818, VSP_001819;
CC Name=3;
CC IsoId=Q8TCU6-3; Sequence=VSP_015090, VSP_015091;
CC -!- TISSUE SPECIFICITY: Mainly expressed in peripheral blood leukocytes and
CC brain. Expressed at intermediate level in spleen and lymph nodes, and
CC weakly expressed in other tissues.
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DR EMBL; AJ320261; CAC86401.1; -; mRNA.
DR EMBL; AL136579; CAB66514.1; -; mRNA.
DR EMBL; AL035106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB037836; BAA92653.2; -; mRNA.
DR EMBL; CH471077; EAW75684.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75685.1; -; Genomic_DNA.
DR EMBL; BC053616; AAH53616.1; -; mRNA.
DR EMBL; AL832913; CAH10614.1; -; mRNA.
DR CCDS; CCDS13410.1; -. [Q8TCU6-1]
DR RefSeq; NP_065871.2; NM_020820.3. [Q8TCU6-1]
DR PDB; 3QIK; X-ray; 2.28 A; A=607-706.
DR PDB; 4YON; X-ray; 1.95 A; A=1-404.
DR PDB; 5D27; X-ray; 1.92 A; A=245-408.
DR PDB; 5D3V; X-ray; 1.85 A; A/B=245-408.
DR PDB; 5D3W; X-ray; 1.85 A; A/B=245-408.
DR PDB; 5D3X; X-ray; 1.69 A; A/B=245-408.
DR PDB; 5D3Y; X-ray; 1.95 A; A/B=245-408.
DR PDB; 5FI0; X-ray; 3.28 A; A/C/E/G=38-408.
DR PDB; 5FI1; X-ray; 3.20 A; A=38-408.
DR PDB; 6PCV; EM; 3.20 A; A=38-1659.
DR PDB; 6VSK; X-ray; 3.12 A; A=409-499.
DR PDBsum; 3QIK; -.
DR PDBsum; 4YON; -.
DR PDBsum; 5D27; -.
DR PDBsum; 5D3V; -.
DR PDBsum; 5D3W; -.
DR PDBsum; 5D3X; -.
DR PDBsum; 5D3Y; -.
DR PDBsum; 5FI0; -.
DR PDBsum; 5FI1; -.
DR PDBsum; 6PCV; -.
DR PDBsum; 6VSK; -.
DR AlphaFoldDB; Q8TCU6; -.
DR SASBDB; Q8TCU6; -.
DR SMR; Q8TCU6; -.
DR BioGRID; 121633; 53.
DR DIP; DIP-46975N; -.
DR IntAct; Q8TCU6; 24.
DR STRING; 9606.ENSP00000361009; -.
DR GlyGen; Q8TCU6; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8TCU6; -.
DR PhosphoSitePlus; Q8TCU6; -.
DR BioMuta; PREX1; -.
DR DMDM; 148886999; -.
DR EPD; Q8TCU6; -.
DR jPOST; Q8TCU6; -.
DR MassIVE; Q8TCU6; -.
DR MaxQB; Q8TCU6; -.
DR PaxDb; Q8TCU6; -.
DR PeptideAtlas; Q8TCU6; -.
DR PRIDE; Q8TCU6; -.
DR ProteomicsDB; 74175; -. [Q8TCU6-1]
DR ProteomicsDB; 74176; -. [Q8TCU6-2]
DR ProteomicsDB; 74177; -. [Q8TCU6-3]
DR Antibodypedia; 1100; 247 antibodies from 35 providers.
DR DNASU; 57580; -.
DR Ensembl; ENST00000371941.4; ENSP00000361009.3; ENSG00000124126.14. [Q8TCU6-1]
DR GeneID; 57580; -.
DR KEGG; hsa:57580; -.
DR MANE-Select; ENST00000371941.4; ENSP00000361009.3; NM_020820.4; NP_065871.3.
DR UCSC; uc002xtw.2; human. [Q8TCU6-1]
DR CTD; 57580; -.
DR DisGeNET; 57580; -.
DR GeneCards; PREX1; -.
DR HGNC; HGNC:32594; PREX1.
DR HPA; ENSG00000124126; Tissue enhanced (bone marrow, brain).
DR MIM; 606905; gene.
DR neXtProt; NX_Q8TCU6; -.
DR OpenTargets; ENSG00000124126; -.
DR PharmGKB; PA164725018; -.
DR VEuPathDB; HostDB:ENSG00000124126; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000159925; -.
DR HOGENOM; CLU_003935_0_0_1; -.
DR InParanoid; Q8TCU6; -.
DR OMA; TMPHYEF; -.
DR OrthoDB; 24217at2759; -.
DR PhylomeDB; Q8TCU6; -.
DR TreeFam; TF328639; -.
DR PathwayCommons; Q8TCU6; -.
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-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q8TCU6; -.
DR SIGNOR; Q8TCU6; -.
DR BioGRID-ORCS; 57580; 31 hits in 1086 CRISPR screens.
DR ChiTaRS; PREX1; human.
DR EvolutionaryTrace; Q8TCU6; -.
DR GeneWiki; PREX1; -.
DR GenomeRNAi; 57580; -.
DR Pharos; Q8TCU6; Tbio.
DR PRO; PR:Q8TCU6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TCU6; protein.
DR Bgee; ENSG00000124126; Expressed in inferior vagus X ganglion and 162 other tissues.
DR ExpressionAtlas; Q8TCU6; baseline and differential.
DR Genevisible; Q8TCU6; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; TAS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; TAS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; TAS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0042119; P:neutrophil activation; TAS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0006801; P:superoxide metabolic process; TAS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1659
FT /note="Phosphatidylinositol 3,4,5-trisphosphate-dependent
FT Rac exchanger 1 protein"
FT /id="PRO_0000080965"
FT DOMAIN 49..240
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 271..392
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 421..496
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 523..597
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 625..703
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK0"
FT MOD_RES 1195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK0"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..703
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_001818"
FT VAR_SEQ 704..708
FT /note="TKAKE -> MGLEQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_001819"
FT VAR_SEQ 1471..1561
FT /note="VLENVEGLPSPGSQAAEDLQQDINAQSLEKVQQYYRKLRAFYLERSNLPTDA
FT STTAVKIDQLIRPINALDELCRLMKSFVHPKPGAAGSVG -> GELQAWGREDHGGRAK
FT ATKHTGSQPPARPRHLPSQCWRTWRGCLLQAARPRRICSRTSTRSPWRKFSSITANSGH
FT FTWSGLTCPRMPAPRR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015090"
FT VAR_SEQ 1562..1659
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015091"
FT VARIANT 659
FT /note="V -> M (in dbSNP:rs55904123)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_061798"
FT VARIANT 696
FT /note="R -> C (in dbSNP:rs7271583)"
FT /id="VAR_057191"
FT VARIANT 786
FT /note="Q -> H (in dbSNP:rs41283558)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_061799"
FT VARIANT 1118
FT /note="A -> T (in dbSNP:rs6012504)"
FT /evidence="ECO:0000269|PubMed:11955434"
FT /id="VAR_057192"
FT VARIANT 1240
FT /note="V -> I (in dbSNP:rs16993997)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_023210"
FT VARIANT 1340
FT /note="K -> E (in dbSNP:rs2664521)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:11955434, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4"
FT /id="VAR_023211"
FT VARIANT 1559
FT /note="S -> T (in dbSNP:rs3936192)"
FT /id="VAR_023212"
FT CONFLICT 910
FT /note="A -> V (in Ref. 2; CAB66514)"
FT /evidence="ECO:0000305"
FT HELIX 36..74
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 144..162
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:4YON"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5FI1"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:4YON"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5FI0"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:5D27"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:5D3X"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5D27"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:5D3X"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:5D3X"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5D3X"
FT HELIX 377..405
FT /evidence="ECO:0007829|PDB:5D3X"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:6VSK"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:6VSK"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:6VSK"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:6VSK"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:6VSK"
FT HELIX 510..521
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 537..544
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 545..555
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 561..573
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 576..584
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 596..602
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 607..620
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 632..642
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:3QIK"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:3QIK"
FT HELIX 681..693
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 698..703
FT /evidence="ECO:0007829|PDB:3QIK"
FT STRAND 706..713
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 720..735
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 739..743
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 750..754
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 765..768
FT /evidence="ECO:0007829|PDB:6PCV"
FT TURN 772..776
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 777..780
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 787..791
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 792..802
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 841..847
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 852..861
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 866..874
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 880..894
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 934..946
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 950..953
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 965..967
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 973..982
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1015..1026
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1319..1346
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1360..1374
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1376..1382
FT /evidence="ECO:0007829|PDB:6PCV"
FT TURN 1386..1388
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1390..1406
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1409..1415
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1419..1423
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1427..1432
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1434..1443
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1445..1449
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1455..1457
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1462..1466
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1481..1517
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1528..1550
FT /evidence="ECO:0007829|PDB:6PCV"
FT TURN 1559..1563
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1564..1574
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1577..1587
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1588..1604
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1613..1622
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 1623..1627
FT /evidence="ECO:0007829|PDB:6PCV"
FT HELIX 1628..1633
FT /evidence="ECO:0007829|PDB:6PCV"
SQ SEQUENCE 1659 AA; 186203 MW; 159419355ED0F00F CRC64;
MEAPSGSEPG GDGAGDCAHP DPRAPGAAAP SSGPGPCAAA RESERQLRLR LCVLNEILGT
ERDYVGTLRF LQSAFLHRIR QNVADSVEKG LTEENVKVLF SNIEDILEVH KDFLAALEYC
LHPEPQSQHE LGNVFLKFKD KFCVYEEYCS NHEKALRLLV ELNKIPTVRA FLLSCMLLGG
RKTTDIPLEG YLLSPIQRIC KYPLLLKELA KRTPGKHPDH PAVQSALQAM KTVCSNINET
KRQMEKLEAL EQLQSHIEGW EGSNLTDICT QLLLQGTLLK ISAGNIQERA FFLFDNLLVY
CKRKSRVTGS KKSTKRTKSI NGSLYIFRGR INTEVMEVEN VEDGTADYHS NGYTVTNGWK
IHNTAKNKWF VCMAKTAEEK QKWLDAIIRE REQRESLKLG MERDAYVMIA EKGEKLYHMM
MNKKVNLIKD RRRKLSTVPK CFLGNEFVAW LLEIGEISKT EEGVNLGQAL LENGIIHHVS
DKHQFKNEQV MYRFRYDDGT YKARSELEDI MSKGVRLYCR LHSLYTPVIK DRDYHLKTYK
SVLPGSKLVD WLLAQGDCQT REEAVALGVG LCNNGFMHHV LEKSEFRDES QYFRFHADEE
MEGTSSKNKQ LRNDFKLVEN ILAKRLLILP QEEDYGFDIE EKNKAVVVKS VQRGSLAEVA
GLQVGRKIYS INEDLVFLRP FSEVESILNQ SFCSRRPLRL LVATKAKEII KIPDQPDTLC
FQIRGAAPPY VYAVGRGSEA MAAGLCAGQC ILKVNGSNVM NDGAPEVLEH FQAFRSRREE
ALGLYQWIYH THEDAQEARA SQEASTEDPS GEQAQEEDQA DSAFPLLSLG PRLSLCEDSP
MVTLTVDNVH LEHGVVYEYV STAGVRCHVL EKIVEPRGCF GLTAKILEAF AANDSVFVEN
CRRLMALSSA IVTMPHFEFR NICDTKLESI GQRIACYQEF AAQLKSRVSP PFKQAPLEPH
PLCGLDFCPT NCHINLMEVS YPKTTPSVGR SFSIRFGRKP SLIGLDPEQG HLNPMSYTQH
CITTMAAPSW KCLPAAEGDP QGQGLHDGSF GPASGTLGQE DRGLSFLLKQ EDREIQDAYL
QLFTKLDVAL KEMKQYVTQI NRLLSTITEP TSGGSCDASL AEEASSLPLV SEESEMDRSD
HGGIKKVCFK VAEEDQEDSG HDTMSYRDSY SECNSNRDSV LSYTSVRSNS SYLGSDEMGS
GDELPCDMRI PSDKQDKLHG CLEHLFNQVD SINALLKGPV MSRAFEETKH FPMNHSLQEF
KQKEECTIRG RSLIQISIQE DPWNLPNSIK TLVDNIQRYV EDGKNQLLLA LLKCTDTELQ
LRRDAIFCQA LVAAVCTFSK QLLAALGYRY NNNGEYEESS RDASRKWLEQ VAATGVLLHC
QSLLSPATVK EERTMLEDIW VTLSELDNVT FSFKQLDENY VANTNVFYHI EGSRQALKVI
FYLDSYHFSK LPSRLEGGAS LRLHTALFTK VLENVEGLPS PGSQAAEDLQ QDINAQSLEK
VQQYYRKLRA FYLERSNLPT DASTTAVKID QLIRPINALD ELCRLMKSFV HPKPGAAGSV
GAGLIPISSE LCYRLGACQM VMCGTGMQRS TLSVSLEQAA ILARSHGLLP KCIMQATDIM
RKQGPRVEIL AKNLRVKDQM PQGAPRLYRL CQPPVDGDL
