ID RPGF2_CANLF Reviewed; 1498 AA.
AC F1PBJ0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Rap guanine nucleotide exchange factor 2;
DE AltName: Full=Cyclic nucleotide ras GEF;
DE Short=CNrasGEF;
DE AltName: Full=Neural RAP guanine nucleotide exchange protein;
DE Short=nRap GEP;
DE AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1;
DE Short=PDZ-GEF1;
DE AltName: Full=RA-GEF-1;
DE AltName: Full=Ras/Rap1-associating GEF-1;
GN Name=RAPGEF2; Synonyms=NRAPGEP, PDZGEF1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP INTERACTION WITH CDH1; CTNNB1 AND TJP1, AND SUBCELLULAR LOCATION.
RX PubMed=10873669; DOI=10.1006/bbrc.2000.3002;
RA Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A.,
RA Kaibuchi K.;
RT "Identification of a novel beta-catenin-interacting protein.";
RL Biochem. Biophys. Res. Commun. 273:712-717(2000).
CC -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF),
CC which activates Rap and Ras family of small GTPases by exchanging bound
CC GDP for free GTP in a cAMP-dependent manner. Serves as a link between
CC cell surface receptors and Rap/Ras GTPases in intracellular signaling
CC cascades. Acts also as an effector for Rap1 by direct association with
CC Rap1-GTP thereby leading to the amplification of Rap1-mediated
CC signaling. Shows weak activity on HRAS. It is controversial whether
CC RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated
CC beta-1 adrenergic receptor ADRB1 leads to the Ras activation through
CC the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and
CC Erk1/2 signaling pathway that leads to sustained inhibition of long
CC term melanogenesis by reducing dendrite extension and melanin
CC synthesis. Provides also inhibitory signals for cell proliferation of
CC melanoma cells and promotes their apoptosis in a cAMP-independent
CC nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-
CC Raf/ERK signaling through a pathway that is independent on both PKA and
CC RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of
CC the major forebrain fiber connections forming the corpus callosum, the
CC anterior commissure and the hippocampal commissure during brain
CC development. Involved in neuronal growth factor (NGF)-induced sustained
CC activation of Rap1 at late endosomes and in brain-derived neurotrophic
CC factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a
CC role in the regulation of embryonic blood vessel formation and in the
CC establishment of basal junction integrity and endothelial barrier
CC function. May be involved in the regulation of the vascular endothelial
CC growth factor receptor KDR and cadherin CDH5 expression at allantois
CC endothelial cell-cell junctions.
CC -!- SUBUNIT: Found in a complex, at least composed of KIDINS220, MAGI2,
CC NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a
CC neuronal growth factor (NGF)-dependent manner. Interacts (via C-
CC terminal domain) with NEDD4 (via WW domains); this interaction leads to
CC ubiquitination and degradation via the proteasome pathway in a cAMP-
CC independent manner. Interacts with MAGI1 (via PDZ domain). Interacts
CC with ADRB1 (via C-terminal PDZ motif); the interaction is direct.
CC Interacts (via Ras-associating domain) with RAP1A (via GTP-bound active
CC form). Interacts weakly with HRAS (via GDP- and GTP-bound forms).
CC Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains)
CC (By similarity). Interacts with CDH1, CTNNB1 and TJP1. {ECO:0000250,
CC ECO:0000269|PubMed:10873669}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:10873669}.
CC Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}.
CC Note=Associated with the synaptic plasma membrane. Localized diffusely
CC in the cytoplasm before neuronal growth factor (NGF) stimulation.
CC Recruited to late endosomes after NGF stimulation. Colocalized with the
CC high affinity nerve growth factor receptor NTRK1 at late endosomes.
CC Translocated to the perinuclear region in a RAP1A-dependent manner.
CC Translocated to the cell membrane (By similarity). Colocalized with
CC CTNNB1 and TJP1 at cell-cell contacts. {ECO:0000250}.
CC -!- DOMAIN: The Ras-associating domain is necessary for the Rap guanine
CC nucleotide exchange activity. The N-terminal regionis necessary for
CC cAMP-binding. The PDZ domain is necessary for its targeting to the cell
CC membrane (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family. {ECO:0000305}.
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DR EMBL; AAEX03010088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003639545.1; XM_003639497.3.
DR AlphaFoldDB; F1PBJ0; -.
DR IntAct; F1PBJ0; 1.
DR STRING; 9615.ENSCAFP00000066461; -.
DR PaxDb; 9612-ENSCAFP00000012838; -.
DR Ensembl; ENSCAFT00000013877.5; ENSCAFP00000012838.3; ENSCAFG00000008719.5.
DR Ensembl; ENSCAFT00040009936.1; ENSCAFP00040008617.1; ENSCAFG00040004820.1.
DR Ensembl; ENSCAFT00805052579; ENSCAFP00805041206; ENSCAFG00805028714.
DR Ensembl; ENSCAFT00845010658.1; ENSCAFP00845008308.1; ENSCAFG00845005844.1.
DR GeneID; 100856359; -.
DR KEGG; cfa:100856359; -.
DR CTD; 9693; -.
DR VEuPathDB; HostDB:ENSCAFG00845005844; -.
DR VGNC; VGNC:45347; RAPGEF2.
DR eggNOG; KOG3542; Eukaryota.
DR GeneTree; ENSGT00940000156418; -.
DR HOGENOM; CLU_002782_0_1_1; -.
DR InParanoid; F1PBJ0; -.
DR OMA; SSHMDQM; -.
DR OrthoDB; 5473909at2759; -.
DR TreeFam; TF313184; -.
DR Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR Proteomes; UP000002254; Chromosome 15.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Chromosome 15.
DR Proteomes; UP000805418; Chromosome 15.
DR Bgee; ENSCAFG00000008719; Expressed in cardiac muscle of left ventricle and 47 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0050699; F:WW domain binding; ISS:UniProtKB.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
DR GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR GO; GO:0021884; P:forebrain neuron development; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0048022; P:negative regulation of melanin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISS:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:1901888; P:regulation of cell junction assembly; ISS:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; ISS:UniProtKB.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01785; RA_PDZ-GEF1; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 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; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR PANTHER; PTHR45161:SF2; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cytoplasm; Developmental protein;
KW Differentiation; Endosome; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1498
FT /note="Rap guanine nucleotide exchange factor 2"
FT /id="PRO_0000423854"
FT DOMAIN 267..380
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 385..468
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 606..692
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 717..944
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 40..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..252
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M386"
FT MOD_RES 644
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F1M386"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M386"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M386"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M386"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHG7"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHG7"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHG7"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M386"
SQ SEQUENCE 1498 AA; 167320 MW; CCA24CD5403DB165 CRC64;
MKPLAIPANH GVMGQQEKHS LPADFTKLHL TDSLHPQVTH VSSSHSGCSI TSDSGSSSLS
DIYQATESEA GDMDLSGLPE TAVDSEDDDD EEDIERASDP LMSRDIVRDC LEKDPIDRTD
DDIEQLLEFM HQLPAFANMT MSVRRELCAV MVFAVVERAG TIVLNDGEEL DSWSVILNGS
VEVTYPDGKA EILCMGNSFG VSPTMDKEYM KGVMRTKVDD CQFVCIAQQD YCRILNQVEK
NMQKVEEEGE IVMVKEHREL DRTGTRKGHI VIKGTSERLT MHLVEEHSVV DPTFIEDFLL
TYRTFLSSPM EVGKKLLEWF NDPSLRDKVT RVVLLWVNNH FNDFEGDPAM TRFLEEFENN
LEREKMGGHL RLLNIACAAK AKRRLMTLTK PSREAPLPFI LLGGSEKGFG IFVDSVDSGS
KATEAGLKRG DQILEVNGQN FENIQLSKAM EILRNNTHLS ITVKTNLFVF KELLTRLSEE
KRNGAPHLPK IGDIKKASRY SIPDLAVDVE QVIGLEKVNK KSKANTVGGR NKLKKILDKT
RISILPQKPY NDIGIGQSQD DSIVGLRQTK HIPTALPVSG TLSSSNPDLL QSHHRILDFS
TTPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPDQY SLCEVSVTPE
GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE DAQELLRESQ ISLLQLSTVE
VATQLSMRNF ELFRNIEPTE YIDDLFKLKS KTSCANLKKF EEVINQETFW VASEILRETN
QLKRMKIIKH FIKIALHCRE CKNFNSMFAI ISGLNLAPVA RLRTTWEKLP NKYEKLFQDL
QDLFDPSRNM AKYRNVLNSQ NLQPPIIPLF PVIKKDLTFL HEGNDSKVDG LVNFEKLRMI
AKEIRHVGRM ASVNMDPALM FRTRKKKWRS LGSLSQGSTN ATVLDVAQTG GHKKRVRRSS
FLNAKKLYED AQMARKVKQY LSNLELEMDE ESLQTLSLQC EPATNTLPKN PGDKKPVKSE
TSPVAPRAGS QQKAQAQPPP PQPQPQHKIN QGLQVPAVSL YPSRKKVPVK DLPPFGINSP
QALKKILSLS EEGSLERHKK QAEDTISNAS SQLSSPPTSP QSSPRKGYTL APSGTVDNFS
DSGHSEISSR SSIVSNSSFD SVPVSLHEER RQRHSVSIVE TNLGVGRMER RTMMEPDQYS
LGSYAPMAES RGLYATATVI SSPSTEELSQ DQGDRASLDA ADSGRGSWTS CSSGSHDNIQ
TIQHQRSWET LPFGHTHFDY SGDPAGLWAS SSHMDQIMFS DHSTKYNRQN QSRESLEQAQ
SRASWASSTG YWGEDSEGDT GTIKRRGGKD VSIEAESSSV TSVTTEETKP VPMPAHVAVT
SSTAKGLIVR KEGRYREPPP TPPGYIGIPI TDFPEGHSHP ARKPPDYNVA LQRSRMVARP
TDTAAPSPIQ QPHGHPASGR PVNKPQWHKP NECDPRLAPY QSQGFSTEED EDEQVSAV
//
