GUC2F_HUMAN
ID GUC2F_HUMAN Reviewed; 1108 AA.
AC P51841; Q9UJF1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Retinal guanylyl cyclase 2;
DE Short=RETGC-2 {ECO:0000303|PubMed:7777544};
DE EC=4.6.1.2 {ECO:0000269|PubMed:7777544};
DE AltName: Full=Guanylate cyclase 2F, retinal {ECO:0000312|HGNC:HGNC:4691};
DE AltName: Full=Guanylate cyclase F;
DE Short=GC-F;
DE AltName: Full=Rod outer segment membrane guanylate cyclase 2;
DE Short=ROS-GC2;
DE Flags: Precursor;
GN Name=GUCY2F; Synonyms=GUC2F, RETGC2;
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 [MRNA], VARIANT GLN-296, TISSUE SPECIFICITY, ACTIVITY
RP REGULATION, AND CATALYTIC ACTIVITY.
RC TISSUE=Retina;
RX PubMed=7777544; DOI=10.1073/pnas.92.12.5535;
RA Lowe D.G., Dizhoor A.M., Liu K., Gu Q., Spencer M., Laura R., Lu L.,
RA Hurley J.B.;
RT "Cloning and expression of a second photoreceptor-specific membrane retina
RT guanylyl cyclase (RetGC), RetGC-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5535-5539(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-10.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [4]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-40; ASN-160; TRP-230; PRO-284; GLN-305;
RP CYS-308; HIS-380; ARG-434; ASP-568; GLN-628; LEU-677; LYS-794; VAL-1010;
RP ARG-1052 AND ASP-1055.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [5]
RP VARIANT ASP-872.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=29515371; DOI=10.3389/fnmol.2018.00052;
RA Wimberg H., Janssen-Bienhold U., Koch K.W.;
RT "Control of the Nucleotide Cycle in Photoreceptor Cell Extracts by Retinal
RT Degeneration Protein 3.";
RL Front. Mol. Neurosci. 11:52-52(2018).
CC -!- FUNCTION: Responsible for the synthesis of cyclic GMP (cGMP) in rods
CC and cones of photoreceptors (PubMed:7777544). Plays an essential role
CC in phototransduction, by mediating cGMP replenishment (By similarity).
CC May also participate in the trafficking of membrane-asociated proteins
CC to the photoreceptor outer segment membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q5SDA5, ECO:0000269|PubMed:7777544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:7777544};
CC -!- ACTIVITY REGULATION: Activated by GUCA1B when free calcium ions
CC concentration is low, and inhibited by GUCA1B when free calcium ions
CC concentration is high (PubMed:15772651). Inhibited by RD3
CC (PubMed:29515371). {ECO:0000269|PubMed:15772651,
CC ECO:0000269|PubMed:29515371}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RD3; promotes the
CC exit of GUCY2F from the endoplasmic reticulum and its trafficking to
CC the photoreceptor outer segments (By similarity).
CC {ECO:0000250|UniProtKB:P51842, ECO:0000250|UniProtKB:Q5SDA5}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC {ECO:0000250|UniProtKB:O02740}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Retina. Localized exclusively in the outer nuclear
CC layer and inner segments of the rod and cone photoreceptor cells.
CC {ECO:0000269|PubMed:7777544}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: There are 9 conserved cysteine residues in sensory guanylate
CC cyclases, 6 in the extracellular domain, which may be involved in
CC intra- or interchain disulfide bonds.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; L37378; AAA74451.1; -; mRNA.
DR EMBL; AL031387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14545.1; -.
DR PIR; I59385; I59385.
DR RefSeq; NP_001513.2; NM_001522.2.
DR AlphaFoldDB; P51841; -.
DR SMR; P51841; -.
DR BioGRID; 109241; 6.
DR IntAct; P51841; 2.
DR MINT; P51841; -.
DR STRING; 9606.ENSP00000218006; -.
DR iPTMnet; P51841; -.
DR PhosphoSitePlus; P51841; -.
DR BioMuta; GUCY2F; -.
DR DMDM; 311033391; -.
DR jPOST; P51841; -.
DR MassIVE; P51841; -.
DR MaxQB; P51841; -.
DR PaxDb; P51841; -.
DR PeptideAtlas; P51841; -.
DR PRIDE; P51841; -.
DR ProteomicsDB; 56431; -.
DR Antibodypedia; 29460; 106 antibodies from 18 providers.
DR DNASU; 2986; -.
DR Ensembl; ENST00000218006.3; ENSP00000218006.2; ENSG00000101890.5.
DR GeneID; 2986; -.
DR KEGG; hsa:2986; -.
DR MANE-Select; ENST00000218006.3; ENSP00000218006.2; NM_001522.3; NP_001513.2.
DR UCSC; uc065aqx.1; human.
DR CTD; 2986; -.
DR DisGeNET; 2986; -.
DR GeneCards; GUCY2F; -.
DR HGNC; HGNC:4691; GUCY2F.
DR HPA; ENSG00000101890; Tissue enriched (retina).
DR MIM; 300041; gene.
DR neXtProt; NX_P51841; -.
DR OpenTargets; ENSG00000101890; -.
DR PharmGKB; PA29071; -.
DR VEuPathDB; HostDB:ENSG00000101890; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000162146; -.
DR HOGENOM; CLU_001072_1_0_1; -.
DR InParanoid; P51841; -.
DR OMA; ICRGGID; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; P51841; -.
DR TreeFam; TF106338; -.
DR BRENDA; 4.6.1.2; 2681.
DR PathwayCommons; P51841; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SignaLink; P51841; -.
DR BioGRID-ORCS; 2986; 9 hits in 718 CRISPR screens.
DR ChiTaRS; GUCY2F; human.
DR GenomeRNAi; 2986; -.
DR Pharos; P51841; Tbio.
DR PRO; PR:P51841; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51841; protein.
DR Bgee; ENSG00000101890; Expressed in right uterine tube and 13 other tissues.
DR Genevisible; P51841; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005640; C:nuclear outer membrane; TAS:ProtInc.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0120200; C:rod photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR033484; GUCY2F.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR11920:SF349; PTHR11920:SF349; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07701; HNOBA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Cell projection; cGMP biosynthesis; Disulfide bond; GTP-binding; Lyase;
KW Membrane; Nucleotide-binding; Reference proteome; Sensory transduction;
KW Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..1108
FT /note="Retinal guanylyl cyclase 2"
FT /id="PRO_0000012386"
FT TOPO_DOM 51..467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..1108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 532..812
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 884..1014
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DISULFID 104..132
FT /evidence="ECO:0000250"
FT DISULFID 452
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 460
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 10
FT /note="R -> P (in a breast cancer sample; somatic mutation;
FT dbSNP:rs755991142)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036419"
FT VARIANT 40
FT /note="S -> C (in dbSNP:rs34228145)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042233"
FT VARIANT 160
FT /note="I -> N (in dbSNP:rs33971675)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042234"
FT VARIANT 230
FT /note="R -> W (in dbSNP:rs33973457)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042235"
FT VARIANT 284
FT /note="L -> P (in dbSNP:rs12008095)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_009136"
FT VARIANT 296
FT /note="R -> Q (in dbSNP:rs502209)"
FT /evidence="ECO:0000269|PubMed:7777544"
FT /id="VAR_009137"
FT VARIANT 305
FT /note="R -> Q (in dbSNP:rs55966326)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042236"
FT VARIANT 308
FT /note="Y -> C (in dbSNP:rs16985750)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030633"
FT VARIANT 380
FT /note="Q -> H (in dbSNP:rs2272925)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030634"
FT VARIANT 434
FT /note="G -> R (in dbSNP:rs56293008)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042237"
FT VARIANT 568
FT /note="G -> D (in a glioblastoma multiforme sample; somatic
FT mutation; dbSNP:rs779221554)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042238"
FT VARIANT 628
FT /note="R -> Q (in dbSNP:rs7883913)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_030635"
FT VARIANT 677
FT /note="V -> L (in dbSNP:rs35474112)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042239"
FT VARIANT 794
FT /note="E -> K (in dbSNP:rs35726803)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042240"
FT VARIANT 872
FT /note="G -> D (in dbSNP:rs148663380)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069424"
FT VARIANT 1010
FT /note="A -> V (in dbSNP:rs55735218)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042241"
FT VARIANT 1052
FT /note="K -> R (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042242"
FT VARIANT 1055
FT /note="E -> D (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042243"
SQ SEQUENCE 1108 AA; 124850 MW; B047BBF1A3C009F9 CRC64;
MFLGLGRFSR LVLWFAAFRK LLGHHGLASA KFLWCLCLLS VMSLPQQVWT LPYKIGVVGP
WACDSLFSKA LPEVAARLAI ERINRDPSFD LSYSFEYVIL NEDCQTSRAL SSFISHHQMA
SGFIGPTNPG YCEAASLLGN SWDKGIFSWA CVNYELDNKI SYPTFSRTLP SPIRVLVTVM
KYFQWAHAGV ISSDEDIWVH TANRVASALR SHGLPVGVVL TTGQDSQSMR KALQRIHQAD
RIRIIIMCMH SALIGGETQM HLLECAHDLK MTDGTYVFVP YDALLYSLPY KHTPYRVLRN
NPKLREAYDA VLTITVESQE KTFYQAFTEA AARGEIPEKL EFDQVSPLFG TIYNSIYFIA
QAMNNAMKEN GQAGAASLVQ HSRNMQFHGF NQLMRTDSNG NGISEYVILD TNLKEWELHS
TYTVDMEMEL LRFGGTPIHF PGGRPPRADA KCWFAEGKIC HGGIDPAFAM MVCLTLLIAL
LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQITSEVQS
GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFSLGD FGDLKSIKSR ASDVFEMMKD
LRHENINPLL GFFYDSGMFA IVTEFCSRGS LEDILTNQDV KLDWMFKSSL LLDLIKGMKY
LHHREFVHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL SEEESSMEEL LWTAPELLRA
PRGSRLGSFA GDVYSFAIIM QEVMVRGTPF CMMDLPAQEI INRLKKPPPV YRPVVPPEHA
PPECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR
ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI
LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
RIHVSLSTVT ILQNLSEGYE VELRGRTELK GKGTEETFWL IGKKGFMKPL PVPPPVDKDG
QVGHGLQPVE IAAFQRRKAE RQLVRNKP
