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   24-JAN-2024, entry version 134.
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   CCDS; CCDS94484.1; -. [Q5JS13-6]
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.
DR   PDB; 3QXL; X-ray; 2.24 A; A/B=23-289.
DR   PDBsum; 3QXL; -.
DR   AlphaFoldDB; Q5JS13; -.
DR   SMR; Q5JS13; -.
DR   BioGRID; 115007; 10.
DR   IntAct; Q5JS13; 4.
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; 9606-ENSP00000259351; -.
DR   PeptideAtlas; 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   Antibodypedia; 30625; 92 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   AGR; HGNC:16851; -.
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; XLSLRIE; -.
DR   OrthoDB; 68574at2759; -.
DR   PhylomeDB; Q5JS13; -.
DR   TreeFam; TF352150; -.
DR   PathwayCommons; Q5JS13; -.
DR   SignaLink; Q5JS13; -.
DR   SIGNOR; Q5JS13; -.
DR   BioGRID-ORCS; 9649; 13 hits in 1150 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 177 other cell types or tissues.
DR   ExpressionAtlas; Q5JS13; baseline and differential.
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:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0032485; P:regulation of Ral protein signal transduction; IDA:FlyBase.
DR   CDD; cd13310; PH_RalGPS1_2; 1.
DR   CDD; cd00155; RasGEF; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 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; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR23113:SF167; RAS-SPECIFIC GUANINE NUCLEOTIDE-RELEASING FACTOR RALGPS1; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48366; Ras GEF; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   Genevisible; Q5JS13; HS.
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
//