RGPS1_HUMAN
ID RGPS1_HUMAN Reviewed; 557 AA.
AC Q5JS13; B4DR86; E9PBQ5; O15059; Q5JT60; Q5JT65; Q5JUG5; Q8N4S6; Q8N5H4;
AC Q8WUV7; Q9NZ16;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ras-specific guanine nucleotide-releasing factor RalGPS1;
DE AltName: Full=Ral GEF with PH domain and SH3-binding motif 1;
DE AltName: Full=Ral guanine nucleotide exchange factor 2;
DE Short=RalGEF 2;
DE AltName: Full=RalA exchange factor RalGPS1;
GN Name=RALGPS1; Synonyms=KIAA0351, RALGEF2;
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), FUNCTION, INTERACTION WITH GRB2;
RP NCK1; PLCG1; RALA AND SRC, AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=10747847; DOI=10.1074/jbc.c000085200;
RA Rebhun J.F., Chen H., Quilliam L.A.;
RT "Identification and characterization of a new family of guanine nucleotide
RT exchange factors for the ras-related GTPase Ral.";
RL J. Biol. Chem. 275:13406-13410(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6).
RC TISSUE=Brain, and Pancreas;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP LEU-148.
RX PubMed=10889189; DOI=10.1074/jbc.m001160200;
RA de Bruyn K.M., de Rooij J., Wolthuis R.M., Rehmann H., Wesenbeek J.,
RA Cool R.H., Wittinghofer A.H., Bos J.L.;
RT "RalGEF2, a pleckstrin homology domain containing guanine nucleotide
RT exchange factor for Ral.";
RL J. Biol. Chem. 275:29761-29766(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 23-289.
RX PubMed=21494904; DOI=10.1007/s13238-011-1036-z;
RA Peng W., Xu J., Guan X., Sun Y., Zhang X.C., Li X., Rao Z.;
RT "Structural study of the Cdc25 domain from Ral-specific guanine-nucleotide
RT exchange factor RalGPS1a.";
RL Protein Cell 2:308-319(2011).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for the small GTPase
CC RALA. May be involved in cytoskeletal organization (By similarity).
CC Guanine nucleotide exchange factor for. {ECO:0000250,
CC ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10889189}.
CC -!- SUBUNIT: Interacts with the SH3 domains of GRB2, NCK1, PLCG1 and SRC.
CC {ECO:0000269|PubMed:10747847}.
CC -!- INTERACTION:
CC Q5JS13-3; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-12217281, EBI-742887;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10889189}. Cell
CC membrane {ECO:0000269|PubMed:10889189}. Note=Associates with membranes
CC through the PH domain.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=RALGPS1B;
CC IsoId=Q5JS13-1; Sequence=Displayed;
CC Name=2; Synonyms=RALGPS1A;
CC IsoId=Q5JS13-2; Sequence=VSP_033478, VSP_033480, VSP_033481;
CC Name=3;
CC IsoId=Q5JS13-3; Sequence=VSP_033475, VSP_033479;
CC Name=4;
CC IsoId=Q5JS13-4; Sequence=VSP_033476, VSP_033477;
CC Name=5;
CC IsoId=Q5JS13-5; Sequence=VSP_033473, VSP_033474;
CC Name=6;
CC IsoId=Q5JS13-6; Sequence=VSP_033471, VSP_033472;
CC Name=7;
CC IsoId=Q5JS13-7; Sequence=VSP_033478, VSP_033481;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Isoform 2 is
CC expressed in brain, colon, kidney, pancreas, prostate, skeletal muscle,
CC small intestine, testis, thymus and uterus. Isoform 1 is expressed at
CC high levels in heart and testis and at lower levels in brain, pancreas,
CC skeletal muscle, small intestine and thymus.
CC {ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10889189}.
CC -!- DOMAIN: The PH domain mediates binding to membranes. It is required for
CC efficient GEF activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19329.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA20808.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF221098; AAF65253.1; -; mRNA.
DR EMBL; AB002349; BAA20808.2; ALT_INIT; mRNA.
DR EMBL; AK299149; BAG61198.1; -; mRNA.
DR EMBL; AL160169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87645.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87646.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87648.1; -; Genomic_DNA.
DR EMBL; BC019329; AAH19329.1; ALT_INIT; mRNA.
DR EMBL; BC032372; AAH32372.1; -; mRNA.
DR EMBL; BC033708; AAH33708.1; -; mRNA.
DR CCDS; CCDS35143.1; -. [Q5JS13-1]
DR CCDS; CCDS55344.1; -. [Q5JS13-4]
DR CCDS; CCDS55345.1; -. [Q5JS13-7]
DR CCDS; CCDS55346.1; -. [Q5JS13-2]
DR RefSeq; NP_001177657.1; NM_001190728.1. [Q5JS13-2]
DR RefSeq; NP_001177658.1; NM_001190729.1. [Q5JS13-7]
DR RefSeq; NP_001177659.1; NM_001190730.1. [Q5JS13-4]
DR RefSeq; NP_001309249.1; NM_001322320.1. [Q5JS13-7]
DR RefSeq; NP_055451.1; NM_014636.2. [Q5JS13-1]
DR RefSeq; XP_016870836.1; XM_017015347.1.
DR RefSeq; XP_016870839.1; XM_017015350.1. [Q5JS13-3]
DR PDB; 3QXL; X-ray; 2.24 A; A/B=23-289.
DR PDBsum; 3QXL; -.
DR AlphaFoldDB; Q5JS13; -.
DR SMR; Q5JS13; -.
DR BioGRID; 115007; 9.
DR IntAct; Q5JS13; 3.
DR MINT; Q5JS13; -.
DR STRING; 9606.ENSP00000259351; -.
DR GlyGen; Q5JS13; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5JS13; -.
DR PhosphoSitePlus; Q5JS13; -.
DR BioMuta; RALGPS1; -.
DR DMDM; 189040074; -.
DR EPD; Q5JS13; -.
DR jPOST; Q5JS13; -.
DR MassIVE; Q5JS13; -.
DR MaxQB; Q5JS13; -.
DR PaxDb; Q5JS13; -.
DR PeptideAtlas; Q5JS13; -.
DR PRIDE; Q5JS13; -.
DR ProteomicsDB; 19273; -.
DR ProteomicsDB; 63124; -. [Q5JS13-1]
DR ProteomicsDB; 63125; -. [Q5JS13-2]
DR ProteomicsDB; 63126; -. [Q5JS13-3]
DR ProteomicsDB; 63127; -. [Q5JS13-4]
DR ProteomicsDB; 63128; -. [Q5JS13-5]
DR ProteomicsDB; 63129; -. [Q5JS13-6]
DR Antibodypedia; 30625; 72 antibodies from 17 providers.
DR DNASU; 9649; -.
DR Ensembl; ENST00000259351.10; ENSP00000259351.5; ENSG00000136828.19. [Q5JS13-1]
DR Ensembl; ENST00000373434.5; ENSP00000362533.1; ENSG00000136828.19. [Q5JS13-2]
DR Ensembl; ENST00000373436.5; ENSP00000362535.1; ENSG00000136828.19. [Q5JS13-4]
DR Ensembl; ENST00000394011.7; ENSP00000377579.3; ENSG00000136828.19. [Q5JS13-6]
DR Ensembl; ENST00000394022.7; ENSP00000377590.3; ENSG00000136828.19. [Q5JS13-3]
DR Ensembl; ENST00000424082.6; ENSP00000415630.2; ENSG00000136828.19. [Q5JS13-7]
DR GeneID; 9649; -.
DR KEGG; hsa:9649; -.
DR MANE-Select; ENST00000259351.10; ENSP00000259351.5; NM_014636.3; NP_055451.1.
DR UCSC; uc004bqo.3; human. [Q5JS13-1]
DR CTD; 9649; -.
DR DisGeNET; 9649; -.
DR GeneCards; RALGPS1; -.
DR HGNC; HGNC:16851; RALGPS1.
DR HPA; ENSG00000136828; Low tissue specificity.
DR MIM; 614444; gene.
DR neXtProt; NX_Q5JS13; -.
DR OpenTargets; ENSG00000136828; -.
DR PharmGKB; PA134907502; -.
DR VEuPathDB; HostDB:ENSG00000136828; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000154079; -.
DR HOGENOM; CLU_021333_0_1_1; -.
DR InParanoid; Q5JS13; -.
DR OMA; GPCICAL; -.
DR OrthoDB; 343666at2759; -.
DR PhylomeDB; Q5JS13; -.
DR TreeFam; TF352150; -.
DR PathwayCommons; Q5JS13; -.
DR SignaLink; Q5JS13; -.
DR SIGNOR; Q5JS13; -.
DR BioGRID-ORCS; 9649; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; RALGPS1; human.
DR GenomeRNAi; 9649; -.
DR Pharos; Q5JS13; Tbio.
DR PRO; PR:Q5JS13; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5JS13; protein.
DR Bgee; ENSG00000136828; Expressed in cortical plate and 175 other tissues.
DR ExpressionAtlas; Q5JS13; baseline and differential.
DR Genevisible; Q5JS13; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0032485; P:regulation of Ral protein signal transduction; IDA:FlyBase.
DR CDD; cd00155; RasGEF; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008937; Ras-like_GEF.
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; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN 1..557
FT /note="Ras-specific guanine nucleotide-releasing factor
FT RalGPS1"
FT /id="PRO_0000333192"
FT DOMAIN 50..289
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 431..543
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 289..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..557
FT /note="Required for stimulation of nucleotide exchange by
FT RALA"
FT MOTIF 330..333
FT /note="PXXP"
FT COMPBIAS 312..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 73..108
FT /note="ELASCGWSKKEKHSLAPNVVAFTRRFNQVSFWVVRE -> KGWPARMEDSLQ
FT KSTVSSRPHDTLQFRKTLPVGPGT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033471"
FT VAR_SEQ 109..557
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033472"
FT VAR_SEQ 205..213
FT /note="IYLLDLIYI -> RSLNWLIFF (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_033473"
FT VAR_SEQ 214..557
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_033474"
FT VAR_SEQ 304..384
FT /note="GPSAGSGSARFSRRPTCPDTSVAGSLPTPPVPRHRKSHSLGNNMMCQLSVVE
FT SKSATFPSEKARHLLDDSVLESRSPRRGL -> VSHLSSLSHQGQAEEARLKPTSGQHP
FT AWMWPSSSRVPAAPPASAAPRSPWPRNLRNDQGQPGAVALTCNPSTLGSRSRRIT (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033475"
FT VAR_SEQ 304..305
FT /note="GP -> AM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033476"
FT VAR_SEQ 306..557
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033477"
FT VAR_SEQ 347..415
FT /note="MMCQLSVVESKSATFPSEKARHLLDDSVLESRSPRRGLALTSSSAVTNGLSL
FT GSSESSEFSEEMSSGLE -> RGRLYATLGPNWRVPVRNSPRTRSCVY (in
FT isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10747847,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_033478"
FT VAR_SEQ 385..557
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033479"
FT VAR_SEQ 483..490
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10747847"
FT /id="VSP_033480"
FT VAR_SEQ 549..557
FT /note="VPANLMSFE -> EAGAAPGPTGTDSHEVDHLEGGAGKEAGPCA (in
FT isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10747847,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_033481"
FT VARIANT 290
FT /note="S -> N (in dbSNP:rs55918931)"
FT /id="VAR_061785"
FT MUTAGEN 148
FT /note="L->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10889189"
FT CONFLICT 86
FT /note="S -> T (in Ref. 6; AAH32372)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="E -> G (in Ref. 3; BAG61198)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="H -> R (in Ref. 3; BAG61198)"
FT /evidence="ECO:0000305"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 89..110
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:3QXL"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:3QXL"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 223..245
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3QXL"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:3QXL"
SQ SEQUENCE 557 AA; 62133 MW; 0C93A55468ED95ED CRC64;
MYKRNGLMAS VLVTSATPQG SSSSDSLEGQ SCDYASKSYD AVVFDVLKVT PEEFASQITL
MDIPVFKAIQ PEELASCGWS KKEKHSLAPN VVAFTRRFNQ VSFWVVREIL TAQTLKIRAE
ILSHFVKIAK KLLELNNLHS LMSVVSALQS APIFRLTKTW ALLNRKDKTT FEKLDYLMSK
EDNYKRTREY IRSLKMVPSI PYLGIYLLDL IYIDSAYPAS GSIMENEQRS NQMNNILRII
ADLQVSCSYD HLTTLPHVQK YLKSVRYIEE LQKFVEDDNY KLSLRIEPGS SSPRLVSSKE
DLAGPSAGSG SARFSRRPTC PDTSVAGSLP TPPVPRHRKS HSLGNNMMCQ LSVVESKSAT
FPSEKARHLL DDSVLESRSP RRGLALTSSS AVTNGLSLGS SESSEFSEEM SSGLESPTGP
CICSLGNSAA VPTMEGPLRR KTLLKEGRKP ALSSWTRYWV ILSGSTLLYY GAKSLRGTDR
KHYKSTPGKK VSIVGWMVQL PDDPEHPDIF QLNNPDKGNV YKFQTGSRFH AILWHKHLDD
ACKSNRPQVP ANLMSFE
