GRP4_HUMAN
ID GRP4_HUMAN Reviewed; 673 AA.
AC Q8TDF6; A6H8M4; C0LTP2; C0LTP3; C0LTP4; C0LTP5; C0LTP7; C9J416; C9JHZ1;
AC Q8N858; Q96QN5; Q96QN6; Q96QN7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=RAS guanyl-releasing protein 4;
GN Name=RASGRP4;
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] (ISOFORMS 1; 2 AND 3), FUNCTION, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND VARIANTS THR-18; LEU-120; ALA-145; CYS-261 AND GLY-335.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11956218; DOI=10.1074/jbc.m202575200;
RA Yang Y., Li L., Wong G.W., Krilis S.A., Madhusudhan M.S., Sali A.,
RA Stevens R.L.;
RT "RasGRP4, a new mast cell-restricted Ras guanine nucleotide-releasing
RT protein with calcium- and diacylglycerol-binding motifs. Identification of
RT defective variants of this signaling protein in asthma, mastocytosis, and
RT mast cell leukemia patients and demonstration of the importance of RasGRP4
RT in mast cell development and function.";
RL J. Biol. Chem. 277:25756-25774(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION,
RP TISSUE SPECIFICITY, AND VARIANT THR-18.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=11880369; DOI=10.1074/jbc.m111330200;
RA Reuther G.W., Lambert Q.T., Rebhun J.F., Caligiuri M.A., Quilliam L.A.,
RA Der C.J.;
RT "RasGRP4 is a novel Ras activator isolated from acute myeloid leukemia.";
RL J. Biol. Chem. 277:30508-30514(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6; 7 AND 8), AND ALTERNATIVE
RP SPLICING.
RX PubMed=21933395; DOI=10.1186/ar3470;
RA Hashimoto T., Yasuda S., Koide H., Kataoka H., Horita T., Atsumi T.,
RA Koike T.;
RT "Aberrant splicing of the hRasGRP4 transcript and decreased levels of this
RT signaling protein in the peripheral blood mononuclear cells in a subset of
RT patients with rheumatoid arthritis.";
RL Arthritis Res. Ther. 13:R154-R154(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-18.
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 [6]
RP FUNCTION.
RX PubMed=12493770; DOI=10.1074/jbc.c200635200;
RA Li L., Yang Y., Stevens R.L.;
RT "RasGRP4 regulates the expression of prostaglandin D2 in human and rat mast
RT cell lines.";
RL J. Biol. Chem. 278:4725-4729(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-548.
RX PubMed=18024961; DOI=10.1074/jbc.m707042200;
RA Katsoulotos G.P., Qi M., Qi J.C., Tanaka K., Hughes W.E., Molloy T.J.,
RA Adachi R., Stevens R.L., Krilis S.A.;
RT "The diacylglycerol-dependent translocation of ras guanine nucleotide-
RT releasing protein 4 inside a human mast cell line results in substantial
RT phenotypic changes, including expression of interleukin 13 receptor
RT alpha2.";
RL J. Biol. Chem. 283:1610-1621(2008).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Functions as a cation- and diacylglycerol (DAG)-regulated
CC nucleotide exchange factor activating Ras through the exchange of bound
CC GDP for GTP. May function in mast cells differentiation.
CC {ECO:0000269|PubMed:11880369, ECO:0000269|PubMed:11956218,
CC ECO:0000269|PubMed:12493770, ECO:0000269|PubMed:18024961}.
CC -!- INTERACTION:
CC Q8TDF6-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-12816371, EBI-752094;
CC Q8TDF6-2; P63167: DYNLL1; NbExp=3; IntAct=EBI-12816371, EBI-349105;
CC Q8TDF6-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12816371, EBI-8652744;
CC Q8TDF6-2; Q9NRS4: TMPRSS4; NbExp=3; IntAct=EBI-12816371, EBI-10313040;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Recruited to
CC membranes upon activation by DAG.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q8TDF6-1; Sequence=Displayed;
CC Name=2; Synonyms=variant 2;
CC IsoId=Q8TDF6-2; Sequence=VSP_030480;
CC Name=3; Synonyms=variant 1;
CC IsoId=Q8TDF6-3; Sequence=VSP_030479;
CC Name=4;
CC IsoId=Q8TDF6-5; Sequence=VSP_043138;
CC Name=5;
CC IsoId=Q8TDF6-6; Sequence=VSP_043176;
CC Name=6;
CC IsoId=Q8TDF6-7; Sequence=VSP_043392;
CC Name=7;
CC IsoId=Q8TDF6-8; Sequence=VSP_046907;
CC Name=8;
CC IsoId=Q8TDF6-9; Sequence=VSP_046908;
CC -!- TISSUE SPECIFICITY: Expressed by mast cells and their progenitors (at
CC protein level). Specifically expressed in mononuclear leukocytes.
CC Highly expressed in myeloid cells compared to lymphoid cells. Also
CC detected in heart, skeletal muscle, spleen, liver, placenta and lung.
CC Not detected in brain. Isoform 1 is the major isoform in normal
CC individuals. Isoform 2 is more significantly expressed in a patient
CC with asthma. Isoform 3 is more significantly expressed in a patient
CC with asthma and a mastocytosis patient. {ECO:0000269|PubMed:11880369,
CC ECO:0000269|PubMed:11956218}.
CC -!- DEVELOPMENTAL STAGE: Expressed early during development. Detected in
CC all fetal tissues tested. {ECO:0000269|PubMed:11956218}.
CC -!- DOMAIN: The phorbol-ester/DAG-type zinc finger mediates the binding and
CC the functional activation by DAG.
CC -!- MISCELLANEOUS: [Isoform 2]: Probably inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Probably inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}.
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DR EMBL; AY048119; AAK85701.1; -; mRNA.
DR EMBL; AY048120; AAK85702.1; -; mRNA.
DR EMBL; AY048121; AAK85703.1; -; mRNA.
DR EMBL; AF448437; AAL87858.1; -; mRNA.
DR EMBL; FJ768677; ACN82414.1; -; mRNA.
DR EMBL; FJ768678; ACN82415.1; -; mRNA.
DR EMBL; FJ768679; ACN82416.1; -; mRNA.
DR EMBL; FJ768680; ACN82417.1; -; mRNA.
DR EMBL; FJ768682; ACN82419.1; -; mRNA.
DR EMBL; AC005789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146669; AAI46670.1; -; mRNA.
DR EMBL; BC150202; AAI50203.1; -; mRNA.
DR CCDS; CCDS46068.1; -. [Q8TDF6-1]
DR CCDS; CCDS54262.1; -. [Q8TDF6-6]
DR CCDS; CCDS54263.1; -. [Q8TDF6-7]
DR CCDS; CCDS54264.1; -. [Q8TDF6-5]
DR CCDS; CCDS59382.1; -. [Q8TDF6-2]
DR CCDS; CCDS59383.1; -. [Q8TDF6-8]
DR CCDS; CCDS59384.1; -. [Q8TDF6-9]
DR RefSeq; NP_001139674.1; NM_001146202.1. [Q8TDF6-2]
DR RefSeq; NP_001139675.1; NM_001146203.1. [Q8TDF6-5]
DR RefSeq; NP_001139676.1; NM_001146204.1. [Q8TDF6-9]
DR RefSeq; NP_001139677.1; NM_001146205.1. [Q8TDF6-8]
DR RefSeq; NP_001139678.1; NM_001146206.1. [Q8TDF6-6]
DR RefSeq; NP_001139679.1; NM_001146207.1. [Q8TDF6-7]
DR RefSeq; NP_733749.1; NM_170604.2. [Q8TDF6-1]
DR PDB; 6AXG; X-ray; 3.30 A; A/C/E/G/I/K=46-460.
DR PDBsum; 6AXG; -.
DR AlphaFoldDB; Q8TDF6; -.
DR SMR; Q8TDF6; -.
DR BioGRID; 125451; 12.
DR IntAct; Q8TDF6; 9.
DR STRING; 9606.ENSP00000479844; -.
DR GlyGen; Q8TDF6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDF6; -.
DR PhosphoSitePlus; Q8TDF6; -.
DR BioMuta; RASGRP4; -.
DR DMDM; 296434529; -.
DR EPD; Q8TDF6; -.
DR MassIVE; Q8TDF6; -.
DR PaxDb; Q8TDF6; -.
DR PeptideAtlas; Q8TDF6; -.
DR PRIDE; Q8TDF6; -.
DR ProteomicsDB; 74276; -. [Q8TDF6-1]
DR ProteomicsDB; 74277; -. [Q8TDF6-2]
DR ProteomicsDB; 74279; -. [Q8TDF6-5]
DR ProteomicsDB; 74280; -. [Q8TDF6-6]
DR ProteomicsDB; 74281; -. [Q8TDF6-7]
DR Antibodypedia; 30068; 81 antibodies from 20 providers.
DR DNASU; 115727; -.
DR Ensembl; ENST00000293062.13; ENSP00000293062.9; ENSG00000171777.16. [Q8TDF6-7]
DR Ensembl; ENST00000426920.6; ENSP00000445966.1; ENSG00000171777.16. [Q8TDF6-6]
DR Ensembl; ENST00000433821.6; ENSP00000411878.2; ENSG00000171777.16. [Q8TDF6-5]
DR Ensembl; ENST00000454404.6; ENSP00000416463.2; ENSG00000171777.16. [Q8TDF6-8]
DR Ensembl; ENST00000586305.5; ENSP00000467604.1; ENSG00000171777.16. [Q8TDF6-2]
DR Ensembl; ENST00000587738.2; ENSP00000465772.1; ENSG00000171777.16. [Q8TDF6-1]
DR Ensembl; ENST00000587753.5; ENSP00000468483.1; ENSG00000171777.16. [Q8TDF6-9]
DR Ensembl; ENST00000589358.5; ENSP00000465742.1; ENSG00000171777.16. [Q8TDF6-1]
DR Ensembl; ENST00000589474.5; ENSP00000466928.1; ENSG00000171777.16. [Q8TDF6-2]
DR Ensembl; ENST00000614135.4; ENSP00000479078.1; ENSG00000171777.16. [Q8TDF6-5]
DR Ensembl; ENST00000615439.5; ENSP00000479844.1; ENSG00000171777.16. [Q8TDF6-1]
DR Ensembl; ENST00000617966.4; ENSP00000479888.1; ENSG00000171777.16. [Q8TDF6-7]
DR Ensembl; ENST00000622174.4; ENSP00000484345.1; ENSG00000171777.16. [Q8TDF6-6]
DR GeneID; 115727; -.
DR KEGG; hsa:115727; -.
DR MANE-Select; ENST00000615439.5; ENSP00000479844.1; NM_170604.3; NP_733749.1.
DR UCSC; uc010efz.4; human. [Q8TDF6-1]
DR CTD; 115727; -.
DR DisGeNET; 115727; -.
DR GeneCards; RASGRP4; -.
DR HGNC; HGNC:18958; RASGRP4.
DR HPA; ENSG00000171777; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 607320; gene.
DR neXtProt; NX_Q8TDF6; -.
DR OpenTargets; ENSG00000171777; -.
DR PharmGKB; PA38770; -.
DR VEuPathDB; HostDB:ENSG00000171777; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000159883; -.
DR HOGENOM; CLU_019261_2_1_1; -.
DR InParanoid; Q8TDF6; -.
DR OMA; LHHAWTQ; -.
DR OrthoDB; 355412at2759; -.
DR PhylomeDB; Q8TDF6; -.
DR PathwayCommons; Q8TDF6; -.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR SignaLink; Q8TDF6; -.
DR BioGRID-ORCS; 115727; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; RASGRP4; human.
DR GenomeRNAi; 115727; -.
DR Pharos; Q8TDF6; Tbio.
DR PRO; PR:Q8TDF6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8TDF6; protein.
DR Bgee; ENSG00000171777; Expressed in granulocyte and 92 other tissues.
DR ExpressionAtlas; Q8TDF6; baseline and differential.
DR Genevisible; Q8TDF6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019992; F:diacylglycerol binding; TAS:UniProtKB.
DR GO; GO:0030742; F:GTP-dependent protein binding; NAS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; NAS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; TAS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0009991; P:response to extracellular stimulus; IDA:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB.
DR CDD; cd00029; C1; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Differentiation; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="RAS guanyl-releasing protein 4"
FT /id="PRO_0000315213"
FT DOMAIN 49..175
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 201..432
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 466..501
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT ZN_FING 540..590
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 171..673
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11956218"
FT /id="VSP_030479"
FT VAR_SEQ 171..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11956218,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030480"
FT VAR_SEQ 221..409
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:21933395"
FT /id="VSP_043176"
FT VAR_SEQ 222..318
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:21933395"
FT /id="VSP_043392"
FT VAR_SEQ 222..255
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:21933395"
FT /id="VSP_046907"
FT VAR_SEQ 319..410
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:21933395"
FT /id="VSP_043138"
FT VAR_SEQ 319..387
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:21933395"
FT /id="VSP_046908"
FT VARIANT 18
FT /note="I -> T (in dbSNP:rs892055)"
FT /evidence="ECO:0000269|PubMed:11880369,
FT ECO:0000269|PubMed:11956218, ECO:0000269|PubMed:15489334"
FT /id="VAR_038144"
FT VARIANT 120
FT /note="Q -> L"
FT /evidence="ECO:0000269|PubMed:11956218"
FT /id="VAR_038145"
FT VARIANT 145
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:11956218"
FT /id="VAR_038146"
FT VARIANT 261
FT /note="R -> C"
FT /evidence="ECO:0000269|PubMed:11956218"
FT /id="VAR_038147"
FT VARIANT 335
FT /note="R -> G (in dbSNP:rs202008979)"
FT /evidence="ECO:0000269|PubMed:11956218"
FT /id="VAR_038148"
FT VARIANT 620
FT /note="E -> K (in dbSNP:rs34377632)"
FT /id="VAR_057172"
FT MUTAGEN 548
FT /note="F->S: Loss of cell membrane targeting."
FT /evidence="ECO:0000269|PubMed:18024961"
FT CONFLICT 27
FT /note="V -> A (in Ref. 1; AAK85703)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="G -> D (in Ref. 1; AAK85703)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="C -> R (in Ref. 1; AAK85703)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="L -> P (in Ref. 1; AAK85701/AAK85703)"
FT /evidence="ECO:0000305"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:6AXG"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:6AXG"
FT TURN 162..167
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 202..218
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 238..259
FT /evidence="ECO:0007829|PDB:6AXG"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:6AXG"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 376..394
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:6AXG"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:6AXG"
SQ SEQUENCE 673 AA; 74882 MW; 3C007F595E3C7A02 CRC64;
MNRKDSKRKS HQECTGKIGG RGRPRQVRRH KTCPSPREIS KVMASMNLGL LSEGGCSEDE
LLEKCIQSFD SAGSLCHEDH MLNMVLAMHS WVLPSADLAA RLLTSYQKAT GDTQELRRLQ
ICHLVRYWLM RHPEVMHQDP QLEEVIGRFW ATVAREGNSA QRRLGDSSDL LSPGGPGPPL
PMSSPGLGKK RKVSLLFDHL ETGELAQHLT YLEFRSFQAI TPQDLRSYVL QGSVRGCPAL
EGSVGLSNSV SRWVQVMVLS RPGPLQRAQV LDKFIHVAQR LHQLQNFNTL MAVTGGLCHS
AISRLKDSHA HLSPDSTKAL LELTELLASH NNYARYRRTW AGCAGFRLPV LGVHLKDLVS
LHEAQPDRLP DGRLHLPKLN NLYLRLQELV ALQGQHPPCS ANEDLLHLLT LSLDLFYTED
EIYELSYARE PRCPKSLPPS PFNAPLVVEW APGVTPKPDR VTLGRHVEQL VESVFKNYDP
EGRGTISQED FERLSGNFPF ACHGLHPPPR QGRGSFSREE LTGYLLRASA ICSKLGLAFL
HTFHEVTFRK PTFCDSCSGF LWGVTKQGYR CRECGLCCHK HCRDQVKVEC KKRPGAKGDA
GPPGAPVPST PAPHASCGSE ENHSYTLSLE PETGCQLRHA WTQTESPHPS WETDTVPCPV
MDPPSTASSK LDS
