ID RFWD3_HUMAN Reviewed; 774 AA.
AC Q6PCD5; A8K585; B2RE35; D3DUJ8; Q5XKR3; Q9H9Q3; Q9NVT4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 10-MAY-2017, entry version 128.
DE RecName: Full=E3 ubiquitin-protein ligase RFWD3;
DE EC=2.3.2.27;
DE AltName: Full=RING finger and WD repeat domain-containing protein 3;
DE AltName: Full=RING finger protein 201;
DE AltName: Full=RING-type E3 ubiquitin transferase RFWD3 {ECO:0000305};
GN Name=RFWD3; Synonyms=RNF201;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma, and Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-564.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-392 AND
RP THR-770.
RC TISSUE=Brain, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-46 AND SER-63, AND MUTAGENESIS OF SER-46;
RP SER-63 AND CYS-315.
RX PubMed=20173098; DOI=10.1073/pnas.0912094107;
RA Fu X., Yucer N., Liu S., Li M., Yi P., Mu J.J., Yang T., Chu J.,
RA Jung S.Y., O'Malley B.W., Gu W., Qin J., Wang Y.;
RT "RFWD3-Mdm2 ubiquitin ligase complex positively regulates p53
RT stability in response to DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4579-4584(2010).
RN [7]
RP FUNCTION, INTERACTION WITH RPA2, AND SUBCELLULAR LOCATION.
RX PubMed=21504906; DOI=10.1074/jbc.M111.222869;
RA Gong Z., Chen J.;
RT "E3 ligase RFWD3 participates in replication checkpoint control.";
RL J. Biol. Chem. 286:22308-22313(2011).
RN [8]
RP FUNCTION, INTERACTION WITH RPA2, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-315.
RX PubMed=21558276; DOI=10.1074/jbc.M111.222802;
RA Liu S., Chu J., Yucer N., Leng M., Wang S.Y., Chen B.P.,
RA Hittelman W.N., Wang Y.;
RT "RING finger and WD repeat domain 3 (RFWD3) associates with
RT replication protein A (RPA) and facilitates RPA-mediated DNA damage
RT response.";
RL J. Biol. Chem. 286:22314-22322(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the
CC ubiquitination of p53/TP53 in the late response to DNA damage, and
CC acts as a positive regulator of p53/TP53 stability, thereby
CC regulating the G1/S DNA damage checkpoint. May act by catalyzing
CC the formation of short polyubiquitin chains on p53/TP53 that are
CC not targeted to the proteasome. In response to ionizing radiation,
CC interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly
CC by restricting MDM2 from extending polyubiquitin chains on
CC ubiquitinated p53/TP53. Plays a role in RPA-mediated DNA damage
CC signaling and repair. {ECO:0000269|PubMed:20173098,
CC ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:21558276}.
CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC protein]-L-lysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with MDM2 and p53/TP53. Binds to the RPA
CC complex via direct interaction with RPA2.
CC {ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21504906,
CC ECO:0000269|PubMed:21558276}.
CC -!- INTERACTION:
CC P61088:UBE2N; NbExp=2; IntAct=EBI-2129159, EBI-1052908;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Cytoplasm.
CC Note=In undamaged cells, found both in the cytoplasm and in the
CC nucleus, partially associated with PML nuclear bodies. In response
CC to replication block, such as that caused by hydroxyurea
CC treatment, or to DNA damage caused by ionizing radiations or
CC doxorubicin, recruited to the nucleus, to stalled replication
CC forks or to sites of DNA repair. This recruitment depends upon
CC RPA2.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in the S-G2 phase.
CC {ECO:0000269|PubMed:21558276}.
CC -!- DOMAIN: The coiled coil domain may be involved in RPA2-binding.
CC -!- PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or
CC ATR. ATM phosphorylation occurs at early times upon DNA damage,
CC while ATR is the major kinase at later times. Phosphorylation by
CC ATM and ATR is required to stabilize p53/TP53. Part of the
CC phosphorylation depends upon RPA2 presence.
CC {ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21558276}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91662.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=BAF83889.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=BAG38132.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; AK001382; BAA91662.1; ALT_INIT; mRNA.
DR EMBL; AK022673; BAB14169.1; -; mRNA.
DR EMBL; AK291200; BAF83889.1; ALT_INIT; mRNA.
DR EMBL; AK315786; BAG38132.1; ALT_INIT; mRNA.
DR EMBL; AC109599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471114; EAW95680.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95681.1; -; Genomic_DNA.
DR EMBL; BC002574; AAH02574.2; -; mRNA.
DR EMBL; BC059371; AAH59371.2; -; mRNA.
DR CCDS; CCDS32486.1; -.
DR RefSeq; NP_060594.3; NM_018124.3.
DR RefSeq; XP_005256078.1; XM_005256021.4.
DR RefSeq; XP_005256079.1; XM_005256022.4.
DR RefSeq; XP_011521493.1; XM_011523191.2.
DR RefSeq; XP_016878880.1; XM_017023391.1.
DR UniGene; Hs.567525; -.
DR ProteinModelPortal; Q6PCD5; -.
DR SMR; Q6PCD5; -.
DR BioGrid; 120460; 51.
DR DIP; DIP-52688N; -.
DR IntAct; Q6PCD5; 39.
DR STRING; 9606.ENSP00000354361; -.
DR iPTMnet; Q6PCD5; -.
DR PhosphoSitePlus; Q6PCD5; -.
DR BioMuta; RFWD3; -.
DR DMDM; 126253679; -.
DR EPD; Q6PCD5; -.
DR MaxQB; Q6PCD5; -.
DR PaxDb; Q6PCD5; -.
DR PeptideAtlas; Q6PCD5; -.
DR PRIDE; Q6PCD5; -.
DR Ensembl; ENST00000361070; ENSP00000354361; ENSG00000168411.
DR Ensembl; ENST00000571750; ENSP00000460049; ENSG00000168411.
DR GeneID; 55159; -.
DR KEGG; hsa:55159; -.
DR UCSC; uc002fda.4; human.
DR CTD; 55159; -.
DR DisGeNET; 55159; -.
DR GeneCards; RFWD3; -.
DR H-InvDB; HIX0013236; -.
DR HGNC; HGNC:25539; RFWD3.
DR HPA; HPA048258; -.
DR HPA; HPA075649; -.
DR MIM; 614151; gene.
DR neXtProt; NX_Q6PCD5; -.
DR OpenTargets; ENSG00000168411; -.
DR PharmGKB; PA134960063; -.
DR eggNOG; KOG1645; Eukaryota.
DR eggNOG; ENOG410XPPE; LUCA.
DR GeneTree; ENSGT00390000008931; -.
DR HOVERGEN; HBG093895; -.
DR InParanoid; Q6PCD5; -.
DR KO; K15691; -.
DR OMA; ILCEFQA; -.
DR OrthoDB; EOG091G05D0; -.
DR PhylomeDB; Q6PCD5; -.
DR TreeFam; TF323359; -.
DR SignaLink; Q6PCD5; -.
DR UniPathway; UPA00143; -.
DR GenomeRNAi; 55159; -.
DR PRO; PR:Q6PCD5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR Bgee; ENSG00000168411; -.
DR CleanEx; HS_RFWD3; -.
DR ExpressionAtlas; Q6PCD5; baseline and differential.
DR Genevisible; Q6PCD5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
DR CDD; cd00162; RING; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway;
KW WD repeat; Zinc; Zinc-finger.
FT CHAIN 1 774 E3 ubiquitin-protein ligase RFWD3.
FT /FTId=PRO_0000278234.
FT REPEAT 495 537 WD 1.
FT REPEAT 539 577 WD 2.
FT REPEAT 583 628 WD 3.
FT ZN_FING 287 331 RING-type; degenerate.
FT {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT COILED 361 413 {ECO:0000255}.
FT MOD_RES 46 46 Phosphoserine; by ATM and ATR.
FT {ECO:0000269|PubMed:20173098}.
FT MOD_RES 63 63 Phosphoserine; by ATM and ATR.
FT {ECO:0000269|PubMed:20173098}.
FT VARIANT 90 90 T -> N (in dbSNP:rs8058922).
FT /FTId=VAR_030700.
FT VARIANT 392 392 R -> K (in dbSNP:rs17854997).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_030701.
FT VARIANT 564 564 I -> V (in dbSNP:rs7193541).
FT {ECO:0000269|Ref.3}.
FT /FTId=VAR_030702.
FT VARIANT 770 770 I -> T (in dbSNP:rs17854996).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_030703.
FT MUTAGEN 46 46 S->A: Markedly decreases phosphorylation
FT following ionizing radiation and
FT abolishes ability to stimulate p53/TP53
FT ubiquitination; when associated with A-
FT 63. {ECO:0000269|PubMed:20173098}.
FT MUTAGEN 63 63 S->A: Markedly decreases phosphorylation
FT following ionizing radiation and
FT abolishes ability to stimulate p53/TP53
FT ubiquitination; when associated with A-
FT 46. {ECO:0000269|PubMed:20173098}.
FT MUTAGEN 315 315 C->A: Abolishes ability to stimulate
FT p53/TP53 ubiquitination. No effect on
FT nuclear localization in response to DNA
FT damage. {ECO:0000269|PubMed:20173098,
FT ECO:0000269|PubMed:21558276}.
FT CONFLICT 221 221 S -> P (in Ref. 1; BAF83889).
FT {ECO:0000305}.
FT CONFLICT 552 552 A -> T (in Ref. 1; BAA91662).
FT {ECO:0000305}.
FT CONFLICT 597 597 A -> V (in Ref. 1; BAA91662).
FT {ECO:0000305}.
FT CONFLICT 741 741 Q -> R (in Ref. 1; BAB14169).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 285 331 ipfam:zf-RING_2 [T]
FT MYHIT 529 568 ismart:WD40 [T]
FT MYHIT 287 331 iprf:ZF_RING_2 [T]
FT MYHIT 486 526 ismart:WD40 [T]
FT MYHIT 733 772 ismart:WD40 [T]
FT MYHIT 287 330 ismart:RING [T]
SQ SEQUENCE 774 AA; 85094 MW; EF6E0E186FD2E580 CRC64;
MAHEAMEYDV QVQLNHAEQQ PAPAGMASSQ GGPALLQPVP ADVVSSQGVP SILQPAPAEV
ISSQATPPLL QPAPQLSVDL TEVEVLGEDT VENINPRTSE QHRQGSDGNH TIPASSLHSM
TNFISGLQRL HGMLEFLRPS SSNHSVGPMR TRRRVSASRR ARAGGSQRTD SARLRAPLDA
YFQVSRTQPD LPATTYDSET RNPVSEELQV SSSSDSDSDS SAEYGGVVDQ AEESGAVILE
EQLAGVSAEQ EVTCIDGGKT LPKQPSPQKS EPLLPSASMD EEEGDTCTIC LEQWTNAGDH
RLSALRCGHL FGYRCISTWL KGQVRKCPQC NKKARHSDIV VLYARTLRAL DTSEQERMKS
SLLKEQMLRK QAELESAQCR LQLQVLTDKC TRLQRRVQDL QKLTSHQSQN LQQPRGSQAW
VLSCSPSSQG QHKHKYHFQK TFTVSQAGNC RIMAYCDALS CLVISQPSPQ ASFLPGFGVK
MLSTANMKSS QYIPMHGKQI RGLAFSSYLR GLLLSASLDN TIKLTSLETN TVVQTYNAGR
PVWSCCWCLD EANYIYAGLA NGSILVYDVR NTSSHVQELV AQKARCPLVS LSYMPRAASA
AFPYGGVLAG TLEDASFWEQ KMDFSHWPHV LPLEPGGCID FQTENSSRHC LVTYRPDKNH
TTIRSVLMEM SYRLDDTGNP ICSCQPVHTF FGGPTCKLLT KNAIFQSPEN DGNILVCTGD
EAANSALLWD AASGSLLQDL QTDQPVLDIC PFEVNRNSYL ATLTEKMVHI YKWE
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