SYTL4_MOUSE
ID SYTL4_MOUSE Reviewed; 673 AA.
AC Q9R0Q1; B1AVI8; B1AVI9; Q8R321; Q9R0Q0;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Synaptotagmin-like protein 4;
DE AltName: Full=Exophilin-2;
DE AltName: Full=Granuphilin;
GN Name=Sytl4; Synonyms=Slp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH PHOSPHOLIPIDS.
RC TISSUE=Pancreas;
RX PubMed=10497219; DOI=10.1074/jbc.274.40.28542;
RA Wang J., Takeuchi T., Yokota H., Izumi T.;
RT "Novel rabphilin-3-like protein associates with insulin-containing granules
RT in pancreatic beta cells.";
RL J. Biol. Chem. 274:28542-28548(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary tumor;
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 [5]
RP INTERACTION WITH RAB27A AND RAB27B.
RX PubMed=11956164; DOI=10.1210/endo.143.5.8823;
RA Zhao S., Torii S., Yokota-Hashimoto H., Takeuchi T., Izumi T.;
RT "Involvement of Rab27b in the regulated secretion of pituitary hormones.";
RL Endocrinology 143:1817-1824(2002).
RN [6]
RP INTERACTION WITH RAB27A.
RX PubMed=11773082; DOI=10.1074/jbc.m112414200;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT functions as a novel Rab27A binding domain.";
RL J. Biol. Chem. 277:9212-9218(2002).
RN [7]
RP MUTAGENESIS OF LEU-43 AND TRP-118, AND INTERACTION WITH RAB27A AND STX1A.
RX PubMed=12101244; DOI=10.1128/mcb.22.15.5518-5526.2002;
RA Torii S., Zhao S., Yi Z., Takeuchi T., Izumi T.;
RT "Granuphilin modulates the exocytosis of secretory granules through
RT interaction with syntaxin 1a.";
RL Mol. Cell. Biol. 22:5518-5526(2002).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLU-14; ILE-18; VAL-21 AND ASP-32, AND INTERACTION
RP WITH RAB27A; STXBP1; RAB3A AND RAB8A.
RX PubMed=12590134; DOI=10.1074/jbc.m213090200;
RA Fukuda M.;
RT "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL J. Biol. Chem. 278:15390-15396(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-275, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH MYO5A.
RX PubMed=23798443; DOI=10.1073/pnas.1306768110;
RA Wei Z., Liu X., Yu C., Zhang M.;
RT "Structural basis of cargo recognitions for class V myosins.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013).
CC -!- FUNCTION: Modulates exocytosis of dense-core granules and secretion of
CC hormones in the pancreas and the pituitary. Interacts with vesicles
CC containing negatively charged phospholipids in a Ca(2+)-independent
CC manner. {ECO:0000269|PubMed:12590134}.
CC -!- SUBUNIT: Part of a ternary complex containing STX1A and RAB27A. Can
CC bind both dominant negative and dominant active mutants of RAB27A.
CC Binds STXBP1, RAB3A, RAB8A and RAB27B. Interacts with MYO5A.
CC {ECO:0000269|PubMed:10497219, ECO:0000269|PubMed:11773082,
CC ECO:0000269|PubMed:11956164, ECO:0000269|PubMed:12101244,
CC ECO:0000269|PubMed:12590134, ECO:0000269|PubMed:23798443}.
CC -!- INTERACTION:
CC Q9R0Q1-1; Q9ERI2: Rab27a; NbExp=2; IntAct=EBI-15734647, EBI-398172;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10497219};
CC Peripheral membrane protein {ECO:0000269|PubMed:10497219}. Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000269|PubMed:10497219};
CC Peripheral membrane protein {ECO:0000269|PubMed:10497219}.
CC Note=Detected close to the plasma membrane and on secretory granules.
CC In pancreas, interacts with insulin-containing vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Granuphilin-a;
CC IsoId=Q9R0Q1-1; Sequence=Displayed;
CC Name=2; Synonyms=Granuphilin-b;
CC IsoId=Q9R0Q1-2; Sequence=VSP_007900, VSP_007901;
CC Name=3;
CC IsoId=Q9R0Q1-3; Sequence=VSP_007902;
CC -!- TISSUE SPECIFICITY: Detected in the pancreatic islet, in particular in
CC insulin-positive beta cells, and in pituitary.
CC {ECO:0000269|PubMed:10497219}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
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DR EMBL; AB025258; BAA84656.1; -; mRNA.
DR EMBL; AB025259; BAA84657.1; -; mRNA.
DR EMBL; AK030401; BAC26945.1; -; mRNA.
DR EMBL; AL691421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026819; AAH26819.1; -; mRNA.
DR CCDS; CCDS30388.1; -. [Q9R0Q1-1]
DR CCDS; CCDS72429.1; -. [Q9R0Q1-2]
DR CCDS; CCDS81169.1; -. [Q9R0Q1-3]
DR RefSeq; NP_001277646.1; NM_001290717.1. [Q9R0Q1-2]
DR RefSeq; NP_001277647.1; NM_001290718.1. [Q9R0Q1-2]
DR RefSeq; NP_001277648.1; NM_001290719.1. [Q9R0Q1-3]
DR RefSeq; NP_038785.1; NM_013757.2. [Q9R0Q1-1]
DR RefSeq; XP_006528614.1; XM_006528551.2. [Q9R0Q1-1]
DR AlphaFoldDB; Q9R0Q1; -.
DR SMR; Q9R0Q1; -.
DR BioGRID; 205168; 2.
DR DIP; DIP-31497N; -.
DR IntAct; Q9R0Q1; 4.
DR STRING; 10090.ENSMUSP00000033608; -.
DR iPTMnet; Q9R0Q1; -.
DR PhosphoSitePlus; Q9R0Q1; -.
DR MaxQB; Q9R0Q1; -.
DR PaxDb; Q9R0Q1; -.
DR PRIDE; Q9R0Q1; -.
DR ProteomicsDB; 254754; -. [Q9R0Q1-1]
DR ProteomicsDB; 254755; -. [Q9R0Q1-2]
DR ProteomicsDB; 254756; -. [Q9R0Q1-3]
DR Antibodypedia; 28523; 189 antibodies from 23 providers.
DR DNASU; 27359; -.
DR Ensembl; ENSMUST00000033608; ENSMUSP00000033608; ENSMUSG00000031255. [Q9R0Q1-1]
DR Ensembl; ENSMUST00000113294; ENSMUSP00000108919; ENSMUSG00000031255. [Q9R0Q1-3]
DR Ensembl; ENSMUST00000113297; ENSMUSP00000108922; ENSMUSG00000031255. [Q9R0Q1-2]
DR GeneID; 27359; -.
DR KEGG; mmu:27359; -.
DR UCSC; uc009ufe.2; mouse. [Q9R0Q1-1]
DR UCSC; uc009uff.2; mouse. [Q9R0Q1-2]
DR UCSC; uc009ufh.3; mouse. [Q9R0Q1-3]
DR CTD; 94121; -.
DR MGI; MGI:1351606; Sytl4.
DR VEuPathDB; HostDB:ENSMUSG00000031255; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000159060; -.
DR HOGENOM; CLU_002711_5_0_1; -.
DR InParanoid; Q9R0Q1; -.
DR OMA; YIPSAKH; -.
DR PhylomeDB; Q9R0Q1; -.
DR TreeFam; TF341184; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 27359; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9R0Q1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R0Q1; protein.
DR Bgee; ENSMUSG00000031255; Expressed in superior cervical ganglion and 152 other tissues.
DR ExpressionAtlas; Q9R0Q1; baseline and differential.
DR Genevisible; Q9R0Q1; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042043; F:neurexin family protein binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IDA:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR GO; GO:0001778; P:plasma membrane repair; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:1905684; P:regulation of plasma membrane repair; ISO:MGI.
DR CDD; cd04029; C2A_SLP-4_5; 1.
DR CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR CDD; cd15764; FYVE_Slp4; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR044134; FYVE_Slp4.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR037303; SLP-4/5_C2A.
DR InterPro; IPR043567; SYTL1-5_C2B.
DR InterPro; IPR028694; SYTL4.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45716:SF4; PTHR45716:SF4; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="Synaptotagmin-like protein 4"
FT /id="PRO_0000190217"
FT DOMAIN 4..122
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 358..480
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 509..635
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 63..105
FT /note="FYVE-type"
FT REGION 184..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C24"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C24"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C24"
FT VAR_SEQ 486..673
FT /note="ISTESSPGLPAHKGELVVSLKYIPASKLPVGGDRKKSKGGEGGELQVWIKEA
FT KNLTAAKSGGTSDSFVKGYLLPMRNKASKRKTPVMKKTLSPHYNHTFVYNGVRLEDLQH
FT MCLELTVWDREPLASNDFLGGVRLGVGTGISNGEVVDWMDSTGEEVSLWQKMRQYPGSW
FT AEGTLQLRSSMVKQKLGV -> VVCFKGRSQLASQVNCL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007902"
FT VAR_SEQ 486..502
FT /note="ISTESSPGLPAHKGELV -> GSVMAKWWTGWIRLVKK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10497219,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007900"
FT VAR_SEQ 503..673
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10497219,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007901"
FT MUTAGEN 14
FT /note="E->A: Abolishes interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:12590134"
FT MUTAGEN 18
FT /note="I->A: Abolishes interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:12590134"
FT MUTAGEN 21
FT /note="V->A: Abolishes interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:12590134"
FT MUTAGEN 32
FT /note="D->A: Abolishes interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:12590134"
FT MUTAGEN 43
FT /note="L->A: Strongly reduces interaction with STX1A."
FT /evidence="ECO:0000269|PubMed:12101244"
FT MUTAGEN 118
FT /note="W->S: Strongly reduces interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:12101244"
SQ SEQUENCE 673 AA; 76021 MW; 2AC218E2A4BE4C8D CRC64;
MSEILDLSFL SEMERDLILG VLQRDEELRK ADEKRIRRLK NELLEIKRKG AKRGSQHYSD
RTCARCQEGL GRLIPKSSTC VGCNHLVCRE CRVLESNGSW RCKVCSKEIE LKKATGDWFY
DQKVNRFDYR TGSEIIRMSL RQKPAVNKRE TAGQSLLQQT QMGDIWPGRR IIQEQQQREQ
SVLFEVPKTR SGKSALEAES ESLDSYTADS DSTSRRDSLD KSGLFPEWKK MSAPKSQVEK
EIPPGNQNAV CGDEGDMVFK KNTKKVLRPS EYTKSVIDLR PEDVAQESGI LGDRSKSVPG
LSVDMEEEEE EEEDIDHLVK LHRQKLARGS MQSGSSMSTL GSIMSIYSEA GDFGNISVTG
KIAFSLKFEQ KTQTLVIHVK ECHQLAYADE AKKRSNPYVK TYLLPDKSRQ GKRKTSIKRD
TINPLYDETF RYEISESLLA QRTLQFSVWH HGRFGRNTFL GEAEVHMDSW KLDKKLDHCL
PLHGKISTES SPGLPAHKGE LVVSLKYIPA SKLPVGGDRK KSKGGEGGEL QVWIKEAKNL
TAAKSGGTSD SFVKGYLLPM RNKASKRKTP VMKKTLSPHY NHTFVYNGVR LEDLQHMCLE
LTVWDREPLA SNDFLGGVRL GVGTGISNGE VVDWMDSTGE EVSLWQKMRQ YPGSWAEGTL
QLRSSMVKQK LGV
