RGL2_HUMAN
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 03-AUG-2022, entry version 183.
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; 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 AlphaFoldDB; O15211; -.
DR SMR; O15211; -.
DR BioGRID; 111801; 21.
DR IntAct; O15211; 20.
DR STRING; 9606.ENSP00000420211; -.
DR iPTMnet; O15211; -.
DR PhosphoSitePlus; O15211; -.
DR BioMuta; RGL2; -.
DR EPD; O15211; -.
DR jPOST; O15211; -.
DR MassIVE; O15211; -.
DR MaxQB; O15211; -.
DR PaxDb; O15211; -.
DR PeptideAtlas; O15211; -.
DR PRIDE; O15211; -.
DR ProteomicsDB; 4111; -.
DR ProteomicsDB; 48511; -. [O15211-1]
DR Antibodypedia; 29066; 196 antibodies from 26 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 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; 940219at2759; -.
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 1076 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 94 other tissues.
DR ExpressionAtlas; O15211; baseline and differential.
DR Genevisible; O15211; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0032485; P:regulation of Ral protein signal transduction; IEA:Ensembl.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 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; IPR030749; RGL2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR PANTHER; PTHR23113:SF213; PTHR23113:SF213; 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; SSF48366; 1.
DR SUPFAM; SSF54236; SSF54236; 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 Alternative splicing; Guanine-nucleotide releasing factor; Phosphoprotein;
KW 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"
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
