ID   RGL2_HUMAN              Reviewed;         777 AA.
AC   O15211; B4DG72; Q5STK0; Q9Y3F3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-OCT-2024, entry version 195.
DE   RecName: Full=Ral guanine nucleotide dissociation stimulator-like 2;
DE            Short=RalGDS-like 2;
DE   AltName: Full=RalGDS-like factor;
DE   AltName: Full=Ras-associated protein RAB2L;
GN   Name=RGL2; Synonyms=RAB2L;
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 [GENOMIC DNA].
RX   PubMed=9545376; DOI=10.1006/jmbi.1998.1637;
RA   Herberg J.A., Beck S., Trowsdale J.;
RT   "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense
RT   cluster at the centromeric end of the MHC.";
RL   J. Mol. Biol. 277:839-857(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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 MRNA] (ISOFORM 2).
RC   TISSUE=Amygdala;
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=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
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] (ISOFORM 1).
RC   TISSUE=Testis;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 656-777 (ISOFORM 1).
RX   PubMed=8976381; DOI=10.1159/000134431;
RA   Isomura M., Okui K., Fujiwara T., Shin S., Nakamura Y.;
RT   "Isolation and mapping of RAB2L, a human cDNA that encodes a protein
RT   homologous to RalGDS.";
RL   Cytogenet. Cell Genet. 74:263-265(1996).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [9]
RP   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 SAMD9.
RX   PubMed=21160498; DOI=10.1038/jid.2010.387;
RA   Hershkovitz D., Gross Y., Nahum S., Yehezkel S., Sarig O., Uitto J.,
RA   Sprecher E.;
RT   "Functional characterization of SAMD9, a protein deficient in
RT   normophosphatemic familial tumoral calcinosis.";
RL   J. Invest. Dermatol. 131:662-669(2011).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-409, AND
RP   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   [12]
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: Probable guanine nucleotide exchange factor. Putative
CC       effector of Ras and/or Rap. Associates with the GTP-bound form of Rap
CC       1A and H-Ras in vitro (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SAMD9. {ECO:0000269|PubMed:21160498}.
CC   -!- INTERACTION:
CC       O15211; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-712355, EBI-10173507;
CC       O15211; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-712355, EBI-3867333;
CC       O15211; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-712355, EBI-739467;
CC       O15211; P01112: HRAS; NbExp=3; IntAct=EBI-712355, EBI-350145;
CC       O15211; Q5T749: KPRP; NbExp=3; IntAct=EBI-712355, EBI-10981970;
CC       O15211; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-712355, EBI-10171774;
CC       O15211; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-712355, EBI-945833;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O15211-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O15211-2; Sequence=VSP_055847, VSP_055848, VSP_055849;
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DR   EMBL; Z97184; CAB09992.1; -; Genomic_DNA.
DR   EMBL; AL050259; CAB43361.1; -; mRNA.
DR   EMBL; AK294442; BAG57683.1; -; mRNA.
DR   EMBL; AL662820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX000343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03709.1; -; Genomic_DNA.
DR   EMBL; BC032681; AAH32681.1; -; mRNA.
DR   EMBL; D85757; BAA75926.1; -; mRNA.
DR   CCDS; CCDS4774.1; -. [O15211-1]
DR   PIR; T08659; T08659.
DR   RefSeq; NP_001230667.1; NM_001243738.1.
DR   RefSeq; NP_004752.1; NM_004761.4. [O15211-1]
DR   PDB; 8AU4; NMR; -; A=643-740.
DR   PDB; 8B69; X-ray; 3.07 A; A/C=643-740.
DR   PDBsum; 8AU4; -.
DR   PDBsum; 8B69; -.
DR   AlphaFoldDB; O15211; -.
DR   SMR; O15211; -.
DR   BioGRID; 111801; 28.
DR   IntAct; O15211; 25.
DR   MINT; O15211; -.
DR   STRING; 9606.ENSP00000420211; -.
DR   iPTMnet; O15211; -.
DR   PhosphoSitePlus; O15211; -.
DR   BioMuta; RGL2; -.
DR   jPOST; O15211; -.
DR   MassIVE; O15211; -.
DR   PaxDb; 9606-ENSP00000420211; -.
DR   PeptideAtlas; O15211; -.
DR   ProteomicsDB; 4111; -.
DR   ProteomicsDB; 48511; -. [O15211-1]
DR   Pumba; O15211; -.
DR   Antibodypedia; 29066; 217 antibodies from 27 providers.
DR   DNASU; 5863; -.
DR   Ensembl; ENST00000383204.8; ENSP00000372691.4; ENSG00000206282.11. [O15211-1]
DR   Ensembl; ENST00000413136.6; ENSP00000407088.2; ENSG00000224841.9. [O15211-1]
DR   Ensembl; ENST00000416548.6; ENSP00000412152.2; ENSG00000228736.9. [O15211-1]
DR   Ensembl; ENST00000452084.6; ENSP00000390098.2; ENSG00000237825.9. [O15211-1]
DR   Ensembl; ENST00000497454.6; ENSP00000420211.1; ENSG00000237441.10. [O15211-1]
DR   GeneID; 5863; -.
DR   KEGG; hsa:5863; -.
DR   MANE-Select; ENST00000497454.6; ENSP00000420211.1; NM_004761.5; NP_004752.1.
DR   UCSC; uc003odv.4; human. [O15211-1]
DR   AGR; HGNC:9769; -.
DR   CTD; 5863; -.
DR   DisGeNET; 5863; -.
DR   GeneCards; RGL2; -.
DR   HGNC; HGNC:9769; RGL2.
DR   HPA; ENSG00000237441; Low tissue specificity.
DR   MIM; 602306; gene.
DR   neXtProt; NX_O15211; -.
DR   OpenTargets; ENSG00000237441; -.
DR   PharmGKB; PA34120; -.
DR   VEuPathDB; HostDB:ENSG00000237441; -.
DR   eggNOG; KOG3629; Eukaryota.
DR   GeneTree; ENSGT00940000161403; -.
DR   HOGENOM; CLU_010252_0_2_1; -.
DR   InParanoid; O15211; -.
DR   OMA; IQQWLRG; -.
DR   OrthoDB; 68574at2759; -.
DR   PhylomeDB; O15211; -.
DR   TreeFam; TF315204; -.
DR   PathwayCommons; O15211; -.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   SignaLink; O15211; -.
DR   BioGRID-ORCS; 5863; 16 hits in 1154 CRISPR screens.
DR   ChiTaRS; RGL2; human.
DR   GeneWiki; RGL2; -.
DR   GenomeRNAi; 5863; -.
DR   Pharos; O15211; Tbio.
DR   PRO; PR:O15211; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O15211; protein.
DR   Bgee; ENSG00000237441; Expressed in spleen and 96 other cell types or tissues.
DR   ExpressionAtlas; O15211; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; NAS:UniProtKB.
DR   GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
DR   GO; GO:0032485; P:regulation of Ral protein signal transduction; IEA:Ensembl.
DR   CDD; cd17211; RA_RGL2; 1.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR23113:SF363; RAL GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR-LIKE 2; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF48366; Ras GEF; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Guanine-nucleotide releasing factor;
KW   Phosphoprotein; Proteomics identification; Reference proteome.
FT   CHAIN           1..777
FT                   /note="Ral guanine nucleotide dissociation stimulator-like
FT                   2"
FT                   /id="PRO_0000068888"
FT   DOMAIN          88..212
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          243..513
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   DOMAIN          648..735
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..82
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055847"
FT   VAR_SEQ         462
FT                   /note="K -> KVSGVSGLDAGLPYPCSRKGRGKSQGSLSFGSCSLRAPSQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055848"
FT   VAR_SEQ         504..777
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055849"
FT   VARIANT         598
FT                   /note="P -> L (in dbSNP:rs34022110)"
FT                   /id="VAR_051903"
FT   VARIANT         705
FT                   /note="G -> E (in dbSNP:rs35273540)"
FT                   /id="VAR_051904"
FT   CONFLICT        503
FT                   /note="S -> R (in Ref. 3; BAG57683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        720
FT                   /note="A -> P (in Ref. 7; BAA75926)"
FT                   /evidence="ECO:0000305"
FT   STRAND          648..655
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   HELIX           659..661
FT                   /evidence="ECO:0007829|PDB:8AU4"
FT   STRAND          662..671
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   HELIX           676..686
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   STRAND          694..696
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   STRAND          698..703
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   TURN            704..706
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   STRAND          707..710
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   HELIX           717..720
FT                   /evidence="ECO:0007829|PDB:8B69"
FT   STRAND          727..731
FT                   /evidence="ECO:0007829|PDB:8B69"
SQ   SEQUENCE   777 AA;  83549 MW;  91AFBAB4D6CEE4A1 CRC64;
     MLPRPLRLLL DTSPPGGVVL SSFRSRDPEE GGGPGGLVVG GGQEEEEEEE EEAPVSVWDE
     EEDGAVFTVT SRQYRPLDPL VPMPPPRSSR RLRAGTLEAL VRHLLDTRTS GTDVSFMSAF
     LATHRAFTST PALLGLMADR LEALESHPTD ELERTTEVAI SVLSTWLASH PEDFGSEAKG
     QLDRLESFLL QTGYAAGKGV GGGSADLIRN LRSRVDPQAP DLPKPLALPG DPPADPTDVL
     VFLADHLAEQ LTLLDAELFL NLIPSQCLGG LWGHRDRPGH SHLCPSVRAT VTQFNKVAGA
     VVSSVLGATS TGEGPGEVTI RPLRPPQRAR LLEKWIRVAE ECRLLRNFSS VYAVVSALQS
     SPIHRLRAAW GEATRDSLRV FSSLCQIFSE EDNYSQSREL LVQEVKLQSP LEPHSKKAPR
     SGSRGGGVVP YLGTFLKDLV MLDAASKDEL ENGYINFDKR RKEFAVLSEL RRLQNECRGY
     NLQPDHDIQR WLQGLRPLTE AQSHRVSCEV EPPGSSDPPA PRVLRPTLVI SQWTEVLGSV
     GVPTPLVSCD RPSTGGDEAP TTPAPLLTRL AQHMKWPSVS SLDSALESSP SLHSPADPSH
     LSPPASSPRP SRGHRRSASC GSPLSGGAEE ASGGTGYGGE GSGPGASDCR IIRVQMELGE
     DGSVYKSILV TSQDKAPSVI SRVLKKNNRD SAVASEYELV QLLPGERELT IPASANVFYA
     MDGASHDFLL RQRRRSSTAT PGVTSGPSAS GTPPSEGGGG SFPRIKATGR KIARALF
//