RNF14_MOUSE
ID RNF14_MOUSE Reviewed; 485 AA.
AC Q9JI90; Q7TPR0; Q9D0L2; Q9D6N2; Q9D6Z8; Q9JI89;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=E3 ubiquitin-protein ligase RNF14;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=Androgen receptor-associated protein 54;
DE AltName: Full=Protein Triad2;
DE AltName: Full=RING finger protein 14;
GN Name=Rnf14; Synonyms=Ara54, Triad2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Van der Reijden B.A., Jansen J.H.;
RT "Identification of a novel TRIAD protein, TRIAD2.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase which accepts
CC ubiquitin from specific E2 ubiquitin-conjugating enzymes and then
CC transfers it to substrates, which could be nuclear proteins. Could play
CC a role as a coactivator for androgen- and, to a lesser extent,
CC progesterone-dependent transcription (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- SUBUNIT: Interacts with the ubiquitin-conjugating enzymes UBE2E1 and
CC UBE2E2. Interacts with AR/androgen receptor; testosterone- and RNF6-
CC regulated it promotes AR transcriptional activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JI90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JI90-2; Sequence=VSP_005751, VSP_005752;
CC -!- DOMAIN: The N-terminal destruction box (D-box) could act as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway. {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger is essential for the interaction with
CC UBE2E2. {ECO:0000250}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- PTM: RING-type zinc finger-dependent and UBE2E2-dependent
CC autoubiquitination. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is one of
CC the conserved features of the family. {ECO:0000305}.
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DR EMBL; AF249667; AAF74266.1; -; mRNA.
DR EMBL; AF249668; AAF74267.1; -; mRNA.
DR EMBL; AK011316; BAB27541.1; -; mRNA.
DR EMBL; AK009783; BAB26503.1; -; mRNA.
DR EMBL; AK010162; BAB26741.1; -; mRNA.
DR EMBL; CH466528; EDL10081.1; -; Genomic_DNA.
DR EMBL; CH466528; EDL10082.1; -; Genomic_DNA.
DR EMBL; CH466528; EDL10083.1; -; Genomic_DNA.
DR EMBL; CH466528; EDL10084.1; -; Genomic_DNA.
DR EMBL; CH466528; EDL10087.1; -; Genomic_DNA.
DR EMBL; BC054841; AAH54841.1; -; mRNA.
DR EMBL; BC094250; AAH94250.1; -; mRNA.
DR CCDS; CCDS29200.1; -. [Q9JI90-1]
DR RefSeq; NP_001158093.1; NM_001164621.1. [Q9JI90-1]
DR RefSeq; NP_001158094.1; NM_001164622.1.
DR RefSeq; NP_064396.2; NM_020012.2. [Q9JI90-1]
DR RefSeq; XP_006526184.1; XM_006526121.2.
DR RefSeq; XP_006526185.1; XM_006526122.2.
DR RefSeq; XP_006526186.1; XM_006526123.2.
DR RefSeq; XP_006526187.1; XM_006526124.2.
DR RefSeq; XP_006526188.1; XM_006526125.2.
DR RefSeq; XP_006526189.1; XM_006526126.1. [Q9JI90-1]
DR RefSeq; XP_006526190.1; XM_006526127.2. [Q9JI90-1]
DR RefSeq; XP_017173444.1; XM_017317955.1.
DR RefSeq; XP_017173445.1; XM_017317956.1. [Q9JI90-1]
DR RefSeq; XP_017173446.1; XM_017317957.1. [Q9JI90-1]
DR AlphaFoldDB; Q9JI90; -.
DR BioGRID; 208150; 11.
DR IntAct; Q9JI90; 8.
DR MINT; Q9JI90; -.
DR STRING; 10090.ENSMUSP00000126205; -.
DR iPTMnet; Q9JI90; -.
DR PhosphoSitePlus; Q9JI90; -.
DR EPD; Q9JI90; -.
DR MaxQB; Q9JI90; -.
DR PaxDb; Q9JI90; -.
DR PeptideAtlas; Q9JI90; -.
DR PRIDE; Q9JI90; -.
DR ProteomicsDB; 300555; -. [Q9JI90-1]
DR ProteomicsDB; 300556; -. [Q9JI90-2]
DR Antibodypedia; 1304; 263 antibodies from 29 providers.
DR DNASU; 56736; -.
DR Ensembl; ENSMUST00000072376; ENSMUSP00000072212; ENSMUSG00000060450. [Q9JI90-1]
DR Ensembl; ENSMUST00000171461; ENSMUSP00000126205; ENSMUSG00000060450. [Q9JI90-1]
DR Ensembl; ENSMUST00000236116; ENSMUSP00000157833; ENSMUSG00000060450. [Q9JI90-1]
DR Ensembl; ENSMUST00000236649; ENSMUSP00000157501; ENSMUSG00000060450. [Q9JI90-2]
DR GeneID; 56736; -.
DR KEGG; mmu:56736; -.
DR UCSC; uc008ese.2; mouse. [Q9JI90-1]
DR CTD; 9604; -.
DR MGI; MGI:1929668; Rnf14.
DR VEuPathDB; HostDB:ENSMUSG00000060450; -.
DR eggNOG; KOG1814; Eukaryota.
DR GeneTree; ENSGT00940000154507; -.
DR HOGENOM; CLU_021364_2_0_1; -.
DR InParanoid; Q9JI90; -.
DR OMA; RVAICED; -.
DR OrthoDB; 1188714at2759; -.
DR PhylomeDB; Q9JI90; -.
DR TreeFam; TF314401; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 56736; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf14; mouse.
DR PRO; PR:Q9JI90; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9JI90; protein.
DR Bgee; ENSMUSG00000060450; Expressed in CA3 field of hippocampus and 274 other tissues.
DR ExpressionAtlas; Q9JI90; baseline and differential.
DR Genevisible; Q9JI90; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR031128; RNF14.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR PANTHER; PTHR11685:SF290; PTHR11685:SF290; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="E3 ubiquitin-protein ligase RNF14"
FT /id="PRO_0000056058"
FT DOMAIN 11..137
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT ZN_FING 221..271
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 290..351
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 405..434
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 217..458
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOTIF 37..45
FT /note="D-box"
FT ACT_SITE 418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS8"
FT VAR_SEQ 52..79
FT /note="GNSNESLQNSGFEYTICFLPPLVLNFEL -> ALCSLQAPRQPVGRTPRQSG
FT AVCLDAVS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_005751"
FT VAR_SEQ 80..485
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_005752"
FT CONFLICT 22
FT /note="A -> V (in Ref. 1; AAF74266/AAF74267)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="G -> R (in Ref. 2; BAB26503)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..106
FT /note="LSAL -> GTLV (in Ref. 2; BAB26503/BAB26741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54926 MW; 6228A9827F16FA47 CRC64;
MSAEDLEAQE DELLALASIY DADEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNESLQN
SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGR
VVLFAWMQFL KEETLTYLNI VSPFELKMGS QKKVQRRATA QASSSTELGV GGAAAADVDQ
EETVDERAVQ DVESLSSLIQ EILDFNQARQ TKCFNSKLFL CSICFCEKLG SDCMYFLECK
HVYCKACLKD YFEIQIKDGQ VKCLNCPEPQ CPSVATPGQV KELVEADLFA RYDRLLLQST
LDLMADVVYC PRPCCQLPVM QEPGGTMAIC SSCNFAFCTL CRLTYHGLSP CKVTAEKLID
LRNEYLQADE ATKRFLEQRY GKRVIQKALE EMESKDWLEK NSKSCPCCGT PIQKLDGCNK
MTCTGCMQYF CWICMGSLSR ANPYRHFTDS ESPCFNRLFH AVDINGDMWE DEIEEDDDDE
DDDDD
