RN207_HUMAN
ID RN207_HUMAN Reviewed; 634 AA.
AC Q6ZRF8; A2VCM8; B4DFR6; Q5TGS6; Q6ZS63; Q96MP2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=RING finger protein 207;
GN Name=RNF207; Synonyms=C1orf188;
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 [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-634 (ISOFORM 1).
RC TISSUE=Amygdala, Brain, Teratocarcinoma, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
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 [4]
RP ASSOCIATION WITH QT INTERVAL VARIANCE.
RX PubMed=19305408; DOI=10.1038/ng.364;
RA Newton-Cheh C., Eijgelsheim M., Rice K.M., de Bakker P.I., Yin X.,
RA Estrada K., Bis J.C., Marciante K., Rivadeneira F., Noseworthy P.A.,
RA Sotoodehnia N., Smith N.L., Rotter J.I., Kors J.A., Witteman J.C.,
RA Hofman A., Heckbert S.R., O'Donnell C.J., Uitterlinden A.G., Psaty B.M.,
RA Lumley T., Larson M.G., Stricker B.H.;
RT "Common variants at ten loci influence QT interval duration in the QTGEN
RT Study.";
RL Nat. Genet. 41:399-406(2009).
RN [5]
RP ASSOCIATION WITH QT INTERVAL VARIANCE, AND VARIANTS SER-573 AND ALA-603.
RX PubMed=19305409; DOI=10.1038/ng.362;
RA Pfeufer A., Sanna S., Arking D.E., Muller M., Gateva V., Fuchsberger C.,
RA Ehret G.B., Orru M., Pattaro C., Kottgen A., Perz S., Usala G.,
RA Barbalic M., Li M., Putz B., Scuteri A., Prineas R.J., Sinner M.F.,
RA Gieger C., Najjar S.S., Kao W.H., Muhleisen T.W., Dei M., Happle C.,
RA Mohlenkamp S., Crisponi L., Erbel R., Jockel K.H., Naitza S., Steinbeck G.,
RA Marroni F., Hicks A.A., Lakatta E., Muller-Myhsok B., Pramstaller P.P.,
RA Wichmann H.E., Schlessinger D., Boerwinkle E., Meitinger T., Uda M.,
RA Coresh J., Kaab S., Abecasis G.R., Chakravarti A.;
RT "Common variants at ten loci modulate the QT interval duration in the QTSCD
RT Study.";
RL Nat. Genet. 41:407-414(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT ALA-603,
RP INTERACTION WITH DNAJA1; HSPA1A; HSPA8 AND KCNH2, AUTOUBIQUITINATION, AND
RP MUTAGENESIS OF CYS-25.
RX PubMed=25281747; DOI=10.1074/jbc.m114.592295;
RA Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
RA Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
RT "RING finger protein RNF207, a novel regulator of cardiac excitation.";
RL J. Biol. Chem. 289:33730-33740(2014).
CC -!- FUNCTION: Plays a role in cardiac repolarization possibly by
CC stabilizing membrane expression of the potassium channel KCNH2/HERG, or
CC by assisting its synthesis, folding or export from the endoplasmic
CC reticulum, in a heat shock protein-dependent manner.
CC {ECO:0000269|PubMed:25281747}.
CC -!- SUBUNIT: Interacts with the core-glycosylated, but not the fully
CC glycosylated form of KCNH2/HERG. Interacts with DNAJA1 and HSPA8.
CC Interacts (via the C-terminus) with HSPA1A; this interaction additively
CC increases KCNH2 expression. {ECO:0000269|PubMed:25281747}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25281747}.
CC Note=Probably located in the endoplasmic reticulum and/or possibly the
CC cis-Golgi apparatus. {ECO:0000269|PubMed:25281747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZRF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZRF8-2; Sequence=VSP_027863, VSP_027864;
CC Name=3;
CC IsoId=Q6ZRF8-3; Sequence=VSP_028439, VSP_028440, VSP_028441;
CC Name=4;
CC IsoId=Q6ZRF8-4; Sequence=VSP_028439, VSP_028442, VSP_028443;
CC -!- POLYMORPHISM: Genetic variation in RNF207 may influence the duration of
CC QT interval, a mesure of cardiac repolarization that depends on
CC multiple environmental and genetic contributors. Prolonged or shortened
CC QT intervals predisposes to ventricular arrhythmias and are a risk
CC factor for sudden cardiac death.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI28238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK056658; BAB71243.1; -; mRNA.
DR EMBL; AK127700; BAC87091.1; -; mRNA.
DR EMBL; AK128246; BAC87352.1; -; mRNA.
DR EMBL; AK294223; BAG57527.1; -; mRNA.
DR EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119780; AAI19781.1; -; mRNA.
DR EMBL; BC128237; AAI28238.1; ALT_INIT; mRNA.
DR CCDS; CCDS59.2; -. [Q6ZRF8-1]
DR RefSeq; NP_997279.2; NM_207396.2. [Q6ZRF8-1]
DR AlphaFoldDB; Q6ZRF8; -.
DR SMR; Q6ZRF8; -.
DR BioGRID; 132764; 4.
DR STRING; 9606.ENSP00000367173; -.
DR iPTMnet; Q6ZRF8; -.
DR PhosphoSitePlus; Q6ZRF8; -.
DR BioMuta; RNF207; -.
DR DMDM; 158563957; -.
DR jPOST; Q6ZRF8; -.
DR MassIVE; Q6ZRF8; -.
DR PaxDb; Q6ZRF8; -.
DR PeptideAtlas; Q6ZRF8; -.
DR PRIDE; Q6ZRF8; -.
DR ProteomicsDB; 68123; -. [Q6ZRF8-1]
DR ProteomicsDB; 68125; -. [Q6ZRF8-3]
DR ProteomicsDB; 68126; -. [Q6ZRF8-4]
DR Antibodypedia; 27241; 112 antibodies from 17 providers.
DR DNASU; 388591; -.
DR Ensembl; ENST00000377939.5; ENSP00000367173.4; ENSG00000158286.13. [Q6ZRF8-1]
DR GeneID; 388591; -.
DR KEGG; hsa:388591; -.
DR MANE-Select; ENST00000377939.5; ENSP00000367173.4; NM_207396.3; NP_997279.2.
DR UCSC; uc001amg.4; human. [Q6ZRF8-1]
DR CTD; 388591; -.
DR DisGeNET; 388591; -.
DR GeneCards; RNF207; -.
DR HGNC; HGNC:32947; RNF207.
DR HPA; ENSG00000158286; Tissue enhanced (heart).
DR MIM; 616923; gene.
DR neXtProt; NX_Q6ZRF8; -.
DR OpenTargets; ENSG00000158286; -.
DR PharmGKB; PA145148144; -.
DR VEuPathDB; HostDB:ENSG00000158286; -.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00510000048612; -.
DR HOGENOM; CLU_034912_0_0_1; -.
DR InParanoid; Q6ZRF8; -.
DR OMA; YEDSYRH; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q6ZRF8; -.
DR TreeFam; TF318184; -.
DR PathwayCommons; Q6ZRF8; -.
DR BioGRID-ORCS; 388591; 15 hits in 1113 CRISPR screens.
DR ChiTaRS; RNF207; human.
DR GenomeRNAi; 388591; -.
DR Pharos; Q6ZRF8; Tbio.
DR PRO; PR:Q6ZRF8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6ZRF8; protein.
DR Bgee; ENSG00000158286; Expressed in apex of heart and 129 other tissues.
DR Genevisible; Q6ZRF8; HS.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0086019; P:cell-cell signaling involved in cardiac conduction; ISS:BHF-UCL.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IGI:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1903954; P:positive regulation of voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISS:BHF-UCL.
DR GO; GO:1903762; P:positive regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISS:BHF-UCL.
DR GO; GO:1901207; P:regulation of heart looping; ISS:BHF-UCL.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039320; RNF207.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22635; PTHR22635; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..634
FT /note="RING finger protein 207"
FT /id="PRO_0000300809"
FT ZN_FING 25..64
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 93..145
FT /note="B box-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 552..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..457
FT /evidence="ECO:0000255"
FT COILED 494..518
FT /evidence="ECO:0000255"
FT COMPBIAS 557..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..227
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028439"
FT VAR_SEQ 109..244
FT /note="DVETTYFCNTCGQPLCARCRDETHRARMFARHDIVALGQRSRDVPQKCTLHA
FT EPYLLFSTDKKLLLCIRCFRDMQKESRAHCVDLESAYVQGCERLEQAVLAVKALQTATR
FT EAIALLQAMVEEVRHSAAEEEDAIH -> AGAAGRVGEEQRVPGCTVPNACTCTQHVFR
FT GRPGSGFSSTSLGHLGPKCEPHYTGGETEVQNKGLEPVSRQWQRLRPFDLGRAHWSPIQ
FT GGVVDLHRRGSPVCRPGPTLKGLCYPSGIEAATAQGRWGQHAVPSGL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027863"
FT VAR_SEQ 245..634
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027864"
FT VAR_SEQ 315..371
FT /note="ELMERLQGIVTRPHHLRPIQSSKIASDHRAEFARCLEPLLLLGPRRVAAAAS
FT GANTL -> AGRGLRPQGADGAPLPLPSRKDVGVTRPKAHAAPVHQHQGAAGGGREHAL
FT RRALPPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028440"
FT VAR_SEQ 372..634
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028441"
FT VAR_SEQ 512..519
FT /note="AQLHDLLQ -> GSRQLAAE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028442"
FT VAR_SEQ 520..634
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028443"
FT VARIANT 421
FT /note="A -> T (in dbSNP:rs12073329)"
FT /id="VAR_052112"
FT VARIANT 539
FT /note="R -> C (in dbSNP:rs55823245)"
FT /id="VAR_061818"
FT VARIANT 573
FT /note="N -> S (in dbSNP:rs709209)"
FT /evidence="ECO:0000269|PubMed:19305409"
FT /id="VAR_052113"
FT VARIANT 603
FT /note="G -> A (associated with prolonged QT interval in
FT heart's electrical cycle; behaves like wild-type in terms
FT of protein expression, subcellular location and shortening
FT of heart's action potential duration, when expressed in
FT neonatal rabbit cardiomyocytes; dbSNP:rs846111)"
FT /evidence="ECO:0000269|PubMed:19305409,
FT ECO:0000269|PubMed:25281747"
FT /id="VAR_052114"
FT MUTAGEN 25
FT /note="C->R: Loss of KCNH2 up-regulation."
FT /evidence="ECO:0000269|PubMed:25281747"
FT CONFLICT 309
FT /note="F -> L (in Ref. 1; BAB71243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 70861 MW; A434507E22D45AFF CRC64;
MSGAIFGPLE GPSSLDAPSI HPLVCPLCHV QYERPCLLDC FHDFCAGCLR GRATDGRLTC
PLCQHQTVLK GPSGLPPVDR LLQFLVDSSG DGVEAVRCAN CDLECSEQDV ETTYFCNTCG
QPLCARCRDE THRARMFARH DIVALGQRSR DVPQKCTLHA EPYLLFSTDK KLLLCIRCFR
DMQKESRAHC VDLESAYVQG CERLEQAVLA VKALQTATRE AIALLQAMVE EVRHSAAEEE
DAIHALFGSM QDRLAERKAL LLQAVQSQYE EKDKAFKEQL SHLATLLPTL QVHLVICSSF
LSLANKAEFL DLGYELMERL QGIVTRPHHL RPIQSSKIAS DHRAEFARCL EPLLLLGPRR
VAAAASGANT LAGGLGPKAL TGPHCPSPVG KMSGSPVQKP TLHRSISTKV LLAEGENTPF
AEHCRHYEDS YRHLQAEMQS LKDQVQELHR DLTKHHSLIK AEIMGDVLHK SLQLDVQIAS
EHASLEGMRV VFQEIWEEAY QRVANEQEIY EAQLHDLLQL RQENAYLTTI TKQITPYVRS
IAKVKERLEP RFQAPVDEQS ESLQNTHDDS RNNAASARNN PGSVPEKREK TSEPKGNSWA
PNGLSEEPLL KNMDHHRSKQ KNGGDVPTWR EHPT
