RN123_HUMAN
ID RN123_HUMAN Reviewed; 1314 AA.
AC Q5XPI4; A1L4Q3; A6NLS5; Q5I022; Q6PFW4; Q71RH0; Q8IW18; Q9H0M8; Q9H5L8;
AC Q9H9T2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=E3 ubiquitin-protein ligase RNF123;
DE EC=2.3.2.27;
DE AltName: Full=Kip1 ubiquitination-promoting complex protein 1;
DE AltName: Full=RING finger protein 123;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF123 {ECO:0000305};
GN Name=RNF123; Synonyms=KPC1; ORFNames=FP1477;
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] (ISOFORM 1), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15531880; DOI=10.1038/ncb1194;
RA Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F., Hatakeyama S.,
RA Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1
RT phase.";
RL Nat. Cell Biol. 6:1229-1235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-854.
RC TISSUE=Brain, Eye, Lung, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 545-1314 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 535-1314 (ISOFORMS 1 AND 2), AND
RP VARIANT HIS-854.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 892-1314 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16227581; DOI=10.1128/mcb.25.21.9292-9303.2005;
RA Hara T., Kamura T., Kotoshiba S., Takahashi H., Fujiwara K., Onoyama I.,
RA Shirakawa M., Mizushima N., Nakayama K.;
RT "Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the
RT cell cycle.";
RL Mol. Cell. Biol. 25:9292-9303(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP FUNCTION, INTERACTION WITH DDX58 AND IFIH1, AND SUBCELLULAR LOCATION.
RX PubMed=27312109; DOI=10.15252/embr.201541703;
RA Wang S., Yang Y.K., Chen T., Zhang H., Yang W.W., Song S.S., Zhai Z.H.,
RA Chen D.Y.;
RT "RNF123 has an E3 ligase-independent function in RIG-I-like receptor-
RT mediated antiviral signaling.";
RL EMBO Rep. 17:1155-1168(2016).
CC -!- FUNCTION: Catalytic subunit of the KPC complex that acts as E3
CC ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-
CC mediated degradation of CDKN1B which is the cyclin-dependent kinase
CC inhibitor at the G0-G1 transition of the cell cycle (PubMed:15531880,
CC PubMed:16227581). Functions also as an inhibitor of innate antiviral
CC signaling mediated by DDX58 and IFIH1 independently of its E3 ligase
CC activity (PubMed:27312109). Interacts with the N-terminal CARD domains
CC of DDX58 and IFIH1 and competes with the downstream adapter MAVS
CC (PubMed:27312109). {ECO:0000269|PubMed:15531880,
CC ECO:0000269|PubMed:16227581, ECO:0000269|PubMed:27312109}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and
CC UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal domain.
CC Interacts with DDX58 (via N-terminus) and IFIH1 (via N-terminus).
CC {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:16227581,
CC ECO:0000269|PubMed:27312109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15531880,
CC ECO:0000269|PubMed:27312109}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XPI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XPI4-2; Sequence=VSP_020650;
CC -!- PTM: Ubiquitinated, leading to its degradation. Deubiquitinated by
CC USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation.
CC {ECO:0000250|UniProtKB:D3ZXK7}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14139.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AY744152; AAU93470.1; -; mRNA.
DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041145; AAH41145.1; -; mRNA.
DR EMBL; BC057392; AAH57392.2; -; mRNA.
DR EMBL; BC088801; AAH88801.1; -; mRNA.
DR EMBL; BC130632; AAI30633.1; -; mRNA.
DR EMBL; AF370367; AAQ15203.1; -; mRNA.
DR EMBL; AK022627; BAB14139.1; ALT_INIT; mRNA.
DR EMBL; AK026968; BAB15607.1; ALT_INIT; mRNA.
DR EMBL; AL136729; CAB66663.2; -; mRNA.
DR CCDS; CCDS33758.1; -. [Q5XPI4-1]
DR RefSeq; NP_071347.2; NM_022064.4. [Q5XPI4-1]
DR RefSeq; XP_006713348.1; XM_006713285.1. [Q5XPI4-1]
DR RefSeq; XP_011532297.1; XM_011533995.1. [Q5XPI4-1]
DR RefSeq; XP_016862507.1; XM_017007018.1. [Q5XPI4-1]
DR PDB; 2MA6; NMR; -; A=1247-1304.
DR PDBsum; 2MA6; -.
DR AlphaFoldDB; Q5XPI4; -.
DR SMR; Q5XPI4; -.
DR BioGRID; 121971; 814.
DR CORUM; Q5XPI4; -.
DR IntAct; Q5XPI4; 37.
DR MINT; Q5XPI4; -.
DR STRING; 9606.ENSP00000328287; -.
DR iPTMnet; Q5XPI4; -.
DR PhosphoSitePlus; Q5XPI4; -.
DR BioMuta; RNF123; -.
DR DMDM; 74748090; -.
DR EPD; Q5XPI4; -.
DR jPOST; Q5XPI4; -.
DR MassIVE; Q5XPI4; -.
DR MaxQB; Q5XPI4; -.
DR PaxDb; Q5XPI4; -.
DR PeptideAtlas; Q5XPI4; -.
DR PRIDE; Q5XPI4; -.
DR ProteomicsDB; 65842; -. [Q5XPI4-1]
DR ProteomicsDB; 65843; -. [Q5XPI4-2]
DR Antibodypedia; 30603; 111 antibodies from 19 providers.
DR DNASU; 63891; -.
DR Ensembl; ENST00000327697.11; ENSP00000328287.6; ENSG00000164068.16. [Q5XPI4-1]
DR GeneID; 63891; -.
DR KEGG; hsa:63891; -.
DR MANE-Select; ENST00000327697.11; ENSP00000328287.6; NM_022064.5; NP_071347.2.
DR UCSC; uc003cxh.5; human. [Q5XPI4-1]
DR CTD; 63891; -.
DR DisGeNET; 63891; -.
DR GeneCards; RNF123; -.
DR HGNC; HGNC:21148; RNF123.
DR HPA; ENSG00000164068; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 614472; gene.
DR neXtProt; NX_Q5XPI4; -.
DR OpenTargets; ENSG00000164068; -.
DR PharmGKB; PA134916827; -.
DR VEuPathDB; HostDB:ENSG00000164068; -.
DR eggNOG; KOG2242; Eukaryota.
DR eggNOG; KOG4692; Eukaryota.
DR GeneTree; ENSGT00940000155781; -.
DR HOGENOM; CLU_006687_2_0_1; -.
DR InParanoid; Q5XPI4; -.
DR OMA; NHQHVMG; -.
DR OrthoDB; 54386at2759; -.
DR PhylomeDB; Q5XPI4; -.
DR TreeFam; TF313546; -.
DR PathwayCommons; Q5XPI4; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q5XPI4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 63891; 73 hits in 1114 CRISPR screens.
DR ChiTaRS; RNF123; human.
DR GeneWiki; RNF123; -.
DR GenomeRNAi; 63891; -.
DR Pharos; Q5XPI4; Tbio.
DR PRO; PR:Q5XPI4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q5XPI4; protein.
DR Bgee; ENSG00000164068; Expressed in hindlimb stylopod muscle and 179 other tissues.
DR ExpressionAtlas; Q5XPI4; baseline and differential.
DR Genevisible; Q5XPI4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd12882; SPRY_RNF123; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035773; SPRY_RNF123.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363; PTHR13363; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1314
FT /note="E3 ubiquitin-protein ligase RNF123"
FT /id="PRO_0000250447"
FT DOMAIN 74..254
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 1254..1292
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZXK7"
FT MOD_RES 683
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5XPI3"
FT VAR_SEQ 1295..1314
FT /note="IVSVEDWEKGANTSTTSSAA -> TSNLLACLYPHWWEPSHGPNCA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020650"
FT VARIANT 51
FT /note="P -> R (in dbSNP:rs2960546)"
FT /id="VAR_027561"
FT VARIANT 387
FT /note="R -> Q (in dbSNP:rs35620248)"
FT /id="VAR_052106"
FT VARIANT 596
FT /note="K -> E (in dbSNP:rs35726701)"
FT /id="VAR_052107"
FT VARIANT 854
FT /note="R -> H (in dbSNP:rs34823813)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_052108"
FT CONFLICT 809
FT /note="K -> R (in Ref. 5; BAB14139)"
FT /evidence="ECO:0000305"
FT STRAND 1250..1253
FT /evidence="ECO:0007829|PDB:2MA6"
FT TURN 1255..1257
FT /evidence="ECO:0007829|PDB:2MA6"
FT STRAND 1258..1261
FT /evidence="ECO:0007829|PDB:2MA6"
FT STRAND 1264..1267
FT /evidence="ECO:0007829|PDB:2MA6"
FT TURN 1268..1270
FT /evidence="ECO:0007829|PDB:2MA6"
FT STRAND 1271..1273
FT /evidence="ECO:0007829|PDB:2MA6"
FT HELIX 1275..1281
FT /evidence="ECO:0007829|PDB:2MA6"
FT TURN 1282..1284
FT /evidence="ECO:0007829|PDB:2MA6"
FT STRAND 1296..1300
FT /evidence="ECO:0007829|PDB:2MA6"
SQ SEQUENCE 1314 AA; 148515 MW; A0F8F4D68EAFB8E1 CRC64;
MASKGAGMSF SRKSYRLTSD AEKSRVTGIV QEKLLNDYLN RIFSSSEHAP PAATSRKPLN
FQNLPEHLDQ LLQVDNEEEE SQGQVEGRLG PSTVVLDHTG GFEGLLLVDD DLLGVIGHSN
FGTIRSTTCV YKGKWLYEVL ISSQGLMQIG WCTISCRFNQ EEGVGDTHNS YAYDGNRVRK
WNVTTTNYGK AWAAGDIVSC LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS
FKESVAFNFG SRPLRYPVAG YRPLQDPPSA DLVRAQRLLG CFRAVLSVEL DPVEGRLLDK
ESSKWRLRGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGIVEKGT PTQAQSVVHQ
VLDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL QIHYLRLTIA ILRHEKSRKF
LLSNVLFDVL RSVVFFYIKS PLRVEEAGLQ ELIPTTWWPH CSSREGKEST EMKEETAEER
LRRRAYERGC QRLRKRIEVV EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS
GRGNMPMLCP PEYMVCFLHR LISALRYYWD EYKASNPHAS FSEEAYIPPQ VFYNGKVDYF
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQSTAMDD LDEDEEPAPA MAQRPMQALA
VGGPLPLPRP GWLSSPTLGR ANRFLSTAAV SLMTPRRPLS TSEKVKVRTL SVEQRTREDI
EGSHWNEGLL LGRPPEEPEQ PLTENSLLEV LDGAVMMYNL SVHQQLGKMV GVSDDVNEYA
MALRDTEDKL RRCPKRRKDI LAELTKSQKV FSEKLDHLSR RLAWVHATVY SQEKMLDIYW
LLRVCLRTIE HGDRTGSLFA FMPEFYLSVA INSYSALKNY FGPVHSMEEL PGYEETLTRL
AAILAKHFAD ARIVGTDIRD SLMQALASYV CYPHSLRAVE RIPEEQRIAM VRNLLAPYEQ
RPWAQTNWIL VRLWRGCGFG YRYTRLPHLL KTKLEDANLP SLQKPCPSTL LQQHMADLLQ
QGPDVAPSFL NSVLNQLNWA FSEFIGMIQE IQQAAERLER NFVDSRQLKV CATCFDLSVS
LLRVLEMTIT LVPEIFLDWT RPTSEMLLRR LAQLLNQVLN RVTAERNLFD RVVTLRLPGL
ESVDHYPILV AVTGILVQLL VRGPASEREQ ATSVLLADPC FQLRSICYLL GQPEPPAPGT
ALPAPDRKRF SLQSYADYIS ADELAQVEQM LAHLTSASAQ AAAASLPTSE EDLCPICYAH
PISAVFQPCG HKSCKACINQ HLMNNKDCFF CKTTIVSVED WEKGANTSTT SSAA
