CYH2_MOUSE
ID CYH2_MOUSE Reviewed; 400 AA.
AC P63034; E9QJX3; O89099; P97695; Q3UP39;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytohesin-2;
DE AltName: Full=ARF nucleotide-binding site opener;
DE Short=Protein ARNO;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 2;
DE Short=CLM2;
DE AltName: Full=SEC7 homolog B;
DE Short=mSec7-2;
GN Name=Cyth2; Synonyms=Pscd2, Sec7b;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=9744817; DOI=10.1016/s0014-5793(98)00937-5;
RA Kim H.-S., Chen Y., Lonai P.;
RT "Complex regulation of multiple cytohesin-like genes in murine tissues and
RT cells.";
RL FEBS Lett. 433:312-316(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu D., Zhang H., Lu J.;
RT "cDNA cloning of mouse cytohesin-2 and demonstration of its association
RT with the integrin beta2 subunit.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Spleen;
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 [4]
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 [5]
RP FUNCTION, DOMAIN, AND AUTOINHIBITION.
RX PubMed=18042453; DOI=10.1016/j.molcel.2007.09.017;
RA DiNitto J.P., Delprato A., Gabe Lee M.T., Cronin T.C., Huang S.,
RA Guilherme A., Czech M.P., Lambright D.G.;
RT "Structural basis and mechanism of autoregulation in 3-phosphoinositide-
RT dependent Grp1 family Arf GTPase exchange factors.";
RL Mol. Cell 28:569-583(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FRMD4A.
RX PubMed=20080746; DOI=10.1073/pnas.0908423107;
RA Ikenouchi J., Umeda M.;
RT "FRMD4A regulates epithelial polarity by connecting Arf6 activation with
RT the PAR complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:748-753(2010).
RN [8]
RP FUNCTION, INTERACTION WITH CCDC120, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25326380; DOI=10.1074/jbc.m114.575787;
RA Torii T., Miyamoto Y., Tago K., Sango K., Nakamura K., Sanbe A., Tanoue A.,
RA Yamauchi J.;
RT "Arf6 guanine nucleotide exchange factor cytohesin-2 binds to CCDC120 and
RT is transported along neurites to mediate neurite growth.";
RL J. Biol. Chem. 289:33887-33903(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 260-378 IN COMPLEXES WITH
RP D-MYO-INOSITOL 1,4,5-TRISPHOSPHATE AND INOSITOL 1,3,4,5-TETRAKISPHOSPHATE,
RP LIPID-BINDING, DOMAIN, AND MUTAGENESIS OF LYS-268; VAL-274; LYS-278;
RP ARG-280; TYR-291; ARG-301; LYS-339 AND HIS-351.
RX PubMed=15359279; DOI=10.1038/sj.emboj.7600388;
RA Cronin T.C., DiNitto J.P., Czech M.P., Lambright D.G.;
RT "Structural determinants of phosphoinositide selectivity in splice variants
RT of Grp1 family PH domains.";
RL EMBO J. 23:3711-3720(2004).
CC -!- FUNCTION: Acts as a guanine-nucleotide exchange factor (GEF). Promotes
CC guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Activates ARF
CC factors through replacement of GDP with GTP (PubMed:18042453). The cell
CC membrane form, in association with ARL4 proteins, recruits ARF6 to the
CC plasma membrane (By similarity). Involved in neurite growth
CC (PubMed:25326380). {ECO:0000250|UniProtKB:Q99418,
CC ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:25326380}.
CC -!- SUBUNIT: Heteromer. Composed of TAMALIN, CYTH2 and at least one GRM1.
CC Interacts with ARRB1. Interacts with ARL4D; the interaction is direct
CC (By similarity). Directly interacts with CCDC120 through the coiled
CC coil domain; this interaction stabilizes CCDC120, possibly by
CC preventing its ubiquitination, and is required for neurite growth in a
CC neuroblastoma cell line (PubMed:25326380). Interacts with FRMD4A
CC (PubMed:20080746). Interacts (via N-terminal domain) with INAVA (via N-
CC terminal domain) (By similarity). {ECO:0000250|UniProtKB:Q99418,
CC ECO:0000269|PubMed:20080746, ECO:0000269|PubMed:25326380}.
CC -!- INTERACTION:
CC P63034; P15920: Atp6v0a2; NbExp=5; IntAct=EBI-988425, EBI-988456;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99418};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q99418}. Cytoplasm
CC {ECO:0000269|PubMed:25326380}. Cell projection
CC {ECO:0000269|PubMed:25326380}. Cell projection, growth cone
CC {ECO:0000269|PubMed:25326380}. Cell junction, tight junction
CC {ECO:0000269|PubMed:20080746}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:20080746}. Note=Recruited to the cell membrane
CC through its association with ARL4A, ARL4C and ARL4D. Requires also
CC interaction with phosphoinositides for targeting to plasma membrane (By
CC similarity). In differentiating neuroblastoma cells, colocalizes with
CC CCDC120 in both neurite shaft and growth cone areas. {ECO:0000250,
CC ECO:0000269|PubMed:25326380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CLM2-A;
CC IsoId=P63034-1, P97695-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P63034-2, P97695-2;
CC Sequence=VSP_006038;
CC Name=3; Synonyms=CLM2-B;
CC IsoId=P63034-3, P97695-3;
CC Sequence=VSP_006037;
CC -!- TISSUE SPECIFICITY: Present in all tissues tested, with highest protein
CC levels in brain and adrenal.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in differentiating neuroblastoma
CC cells. {ECO:0000269|PubMed:25326380}.
CC -!- DOMAIN: Binds via its PH domain to the inositol head group of
CC phosphatidylinositol 3,4,5-trisphosphate. The PH domain is necessary
CC and sufficient for plasma membrane relocalization (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domain is involved in interaction with CCDC120.
CC {ECO:0000269|PubMed:25326380}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB013466; BAA33429.1; -; mRNA.
DR EMBL; AB013467; BAA33430.1; -; mRNA.
DR EMBL; AB013469; BAA33431.1; -; Genomic_DNA.
DR EMBL; AB013469; BAA33432.1; -; Genomic_DNA.
DR EMBL; AF079971; AAC77924.1; -; mRNA.
DR EMBL; AK045451; BAC32376.1; -; mRNA.
DR EMBL; AK143829; BAE25558.1; -; mRNA.
DR EMBL; AC149053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52249.1; -. [P63034-2]
DR RefSeq; NP_001106171.1; NM_001112701.1.
DR RefSeq; NP_035311.1; NM_011181.3.
DR PDB; 1U27; X-ray; 2.30 A; A=260-378.
DR PDB; 1U29; X-ray; 1.80 A; A=260-378.
DR PDBsum; 1U27; -.
DR PDBsum; 1U29; -.
DR AlphaFoldDB; P63034; -.
DR BMRB; P63034; -.
DR SASBDB; P63034; -.
DR SMR; P63034; -.
DR BioGRID; 202412; 11.
DR CORUM; P63034; -.
DR IntAct; P63034; 3.
DR MINT; P63034; -.
DR STRING; 10090.ENSMUSP00000103357; -.
DR iPTMnet; P63034; -.
DR PhosphoSitePlus; P63034; -.
DR EPD; P63034; -.
DR MaxQB; P63034; -.
DR PaxDb; P63034; -.
DR PRIDE; P63034; -.
DR ProteomicsDB; 285440; -.
DR ProteomicsDB; 285441; -. [P63034-2]
DR ProteomicsDB; 285442; -. [P63034-3]
DR Antibodypedia; 4437; 300 antibodies from 33 providers.
DR DNASU; 19158; -.
DR Ensembl; ENSMUST00000056820; ENSMUSP00000051423; ENSMUSG00000003269. [P63034-1]
DR GeneID; 19158; -.
DR KEGG; mmu:19158; -.
DR UCSC; uc009gxf.2; mouse.
DR CTD; 9266; -.
DR MGI; MGI:1334255; Cyth2.
DR VEuPathDB; HostDB:ENSMUSG00000003269; -.
DR eggNOG; KOG0930; Eukaryota.
DR GeneTree; ENSGT00940000160074; -.
DR InParanoid; P63034; -.
DR OrthoDB; 657055at2759; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR BioGRID-ORCS; 19158; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Cyth2; mouse.
DR EvolutionaryTrace; P63034; -.
DR PRO; PR:P63034; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P63034; protein.
DR Bgee; ENSMUSG00000003269; Expressed in cortical plate and 262 other tissues.
DR ExpressionAtlas; P63034; baseline and differential.
DR Genevisible; P63034; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098892; C:extrinsic component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Reference proteome; Tight junction.
FT CHAIN 1..400
FT /note="Cytohesin-2"
FT /id="PRO_0000120198"
FT DOMAIN 72..201
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 259..376
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 387..395
FT /note="C-terminal autoinhibitory region"
FT /evidence="ECO:0000250"
FT COILED 10..67
FT /evidence="ECO:0000255"
FT BINDING 268..276
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT BINDING 280
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000269|PubMed:15359279"
FT BINDING 291
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000269|PubMed:15359279"
FT BINDING 301
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000269|PubMed:15359279"
FT BINDING 339
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000269|PubMed:15359279"
FT BINDING 350
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000269|PubMed:15359279"
FT BINDING 351
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000269|PubMed:15359279"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9744817"
FT /id="VSP_006037"
FT VAR_SEQ 273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006038"
FT MUTAGEN 268
FT /note="K->A: Abolishes phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 274
FT /note="V->G: Increased phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 278
FT /note="K->A: Strongly reduces phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 280
FT /note="R->A: Abolishes phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 291
FT /note="Y->F: Abolishes phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 301
FT /note="R->A: Abolishes phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 339
FT /note="K->A: Abolishes phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT MUTAGEN 351
FT /note="H->A: Abolishes phosphatidylinositol 3,4,5-
FT trisphosphate binding."
FT /evidence="ECO:0000269|PubMed:15359279"
FT CONFLICT 270
FT /note="A -> G (in Ref. 1; BAA33429/BAA33430/BAA33431/
FT BAA33432, 2; AAC77924/BAC32376 and 3; BAE25558)"
FT /evidence="ECO:0000305"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1U29"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:1U29"
FT HELIX 361..376
FT /evidence="ECO:0007829|PDB:1U29"
SQ SEQUENCE 400 AA; 46585 MW; 8F6F4F7C2F931A89 CRC64;
MEDGVYEPPD LTPEERMELE NIRRRKQELL VEIQRLREEL SEAMSEVEGL EANEGSKTLQ
RNRKMAMGRK KFNMDPKKGI QFLVEHELLQ NTPEEIARFL YKGEGLNKTA IGDYLGEREE
LNLSVLHAFV DLHEFTDLNL VQALRQFLWS FRLPGEAQKI DRMMEAFAQR YCLCNPGVFQ
STDTCYVLSF AVIMLNTSLH NPNVRDKPGL ERFVAMNRGI NEGGDLPEDL LRNLYDSIRN
EPFKIPEDDG NDLTHTFFNP DREGWLLKLA GGRVKTWKRR WFILTDNCLY YFEYTTDKEP
RGIIPLENLS IREVDDPRKP NCFELYIPNN KGQLIKACKT EADGRVVEGN HMVYRISAPT
QEEKDEWIKS IQAAVSVDPF YEMLAARKKR ISVKKKQEQP
