UTP4_HUMAN
ID UTP4_HUMAN Reviewed; 686 AA.
AC Q969X6; Q8NCD9; Q8TF14; Q96SP0; Q96SR9; Q96SZ9; Q96T13; Q9BWK6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=U3 small nucleolar RNA-associated protein 4 homolog;
DE AltName: Full=Cirhin;
DE AltName: Full=UTP4 small subunit processome component;
GN Name=UTP4 {ECO:0000312|HGNC:HGNC:1983};
GN Synonyms=CIRH1A, cPERP-E {ECO:0000303|PubMed:20813266}, KIAA1988;
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] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 95-686 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 444-686 (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Placenta;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT TRP-565.
RX PubMed=16225863; DOI=10.1016/j.yexcr.2005.08.012;
RA Yu B., Mitchell G.A., Richter A.;
RT "Nucleolar localization of cirhin, the protein mutated in North American
RT Indian childhood cirrhosis.";
RL Exp. Cell Res. 311:218-228(2005).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17699751; DOI=10.1101/gad.436707;
RA Prieto J.L., McStay B.;
RT "Recruitment of factors linking transcription and processing of pre-rRNA to
RT NOR chromatin is UBF-dependent and occurs independent of transcription in
RT human cells.";
RL Genes Dev. 21:2041-2054(2007).
RN [7]
RP FUNCTION, INTERACTION WITH HIVEP1, AND CHARACTERIZATION OF VARIANT TRP-565.
RX PubMed=19732766; DOI=10.1016/j.yexcr.2009.08.017;
RA Yu B., Mitchell G.A., Richter A.;
RT "Cirhin up-regulates a canonical NF-kappaB element through strong
RT interaction with Cirip/HIVEP1.";
RL Exp. Cell Res. 315:3086-3098(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [9]
RP FUNCTION, INTERACTION WITH NOL11, AND POSSIBLE ASSOCIATION IN THE SSU
RP PROCESSOME T-UTP SUBCOMPLEX.
RX PubMed=22916032; DOI=10.1371/journal.pgen.1002892;
RA Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.;
RT "NOL11, implicated in the pathogenesis of North American Indian childhood
RT cirrhosis, is required for pre-rRNA transcription and processing.";
RL PLoS Genet. 8:E1002892-E1002892(2012).
RN [10]
RP SUBCELLULAR LOCATION, INTERACTION WITH UTP15 AND WDR43, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=24219289; DOI=10.1139/bcb-2013-0062;
RA Sato M., Araki N., Kumeta M., Takeyasu K., Taguchi Y., Asai T.,
RA Furukawa K., Horigome T.;
RT "Interaction, mobility, and phosphorylation of human orthologues of WD
RT repeat-containing components of the yeast SSU processome t-UTP sub-
RT complex.";
RL Biochem. Cell Biol. 91:466-475(2013).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP VARIANT TRP-565.
RX PubMed=12417987; DOI=10.1086/344580;
RA Chagnon P., Michaud J., Mitchell G., Mercier J., Marion J.-F., Drouin E.,
RA Rasquin-Weber A., Hudson T.J., Richter A.;
RT "A missense mutation (R565W) in cirhin (FLJ14728) in North American Indian
RT childhood cirrhosis.";
RL Am. J. Hum. Genet. 71:1443-1449(2002).
RN [13]
RP VARIANT TRP-565.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing
CC of pre-18S ribosomal RNA. Involved in small subunit (SSU) pre-rRNA
CC processing at sites A', A0, 1 and 2b. Required for optimal pre-
CC ribosomal RNA transcription by RNA polymerase (PubMed:17699751,
CC PubMed:19732766). May be a transcriptional regulator. Acts as a
CC positive regulator of HIVEP1 which specifically binds to the DNA
CC sequence 5'-GGGACTTTCC-3' found in enhancer elements of numerous viral
CC promoters such as those of HIV-1, SV40, or CMV (PubMed:19732766).
CC {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:19732766,
CC ECO:0000269|PubMed:22916032}.
CC -!- SUBUNIT: Interacts with HIVEP1 (PubMed:19732766) Interacts with NOL11
CC (PubMed:22916032). Interacts directly with UTP15 and WDR43
CC (PubMed:24219289). May be a component of the proposed t-UTP subcomplex
CC of the ribosomal small subunit (SSU) processome containing at least
CC UTP4, WDR43, HEATR1, UTP15, WDR75 (PubMed:17699751, PubMed:22916032).
CC {ECO:0000269|PubMed:19732766, ECO:0000269|PubMed:22916032,
CC ECO:0000269|PubMed:24219289, ECO:0000305|PubMed:17699751}.
CC -!- INTERACTION:
CC Q969X6; P15822: HIVEP1; NbExp=3; IntAct=EBI-2602591, EBI-722264;
CC Q969X6; Q9H8H0: NOL11; NbExp=6; IntAct=EBI-2602591, EBI-725885;
CC Q969X6; Q8TED0: UTP15; NbExp=3; IntAct=EBI-2602591, EBI-1048301;
CC Q969X6; Q15061: WDR43; NbExp=3; IntAct=EBI-2602591, EBI-2563523;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:16225863, ECO:0000269|PubMed:24219289}. Chromosome
CC {ECO:0000269|PubMed:20813266}. Note=Found predominantly at the
CC fibrillar center. {ECO:0000269|PubMed:24219289}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q969X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969X6-2; Sequence=VSP_009201;
CC Name=3;
CC IsoId=Q969X6-3; Sequence=VSP_009202, VSP_009203;
CC -!- PTM: May be phosphorylated during mitosis; may control the association
CC of this protein with WRD43 and UTP15. {ECO:0000269|PubMed:24219289}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55100.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55116.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB85574.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB075868; BAB85574.2; ALT_INIT; mRNA.
DR EMBL; AK027419; BAB55100.1; ALT_INIT; mRNA.
DR EMBL; AK027445; BAB55116.1; ALT_INIT; mRNA.
DR EMBL; AK027584; BAB55212.1; ALT_INIT; mRNA.
DR EMBL; AK027634; BAB55251.1; -; mRNA.
DR EMBL; AK027675; BAB55287.1; -; mRNA.
DR EMBL; AK074795; BAC11214.1; -; mRNA.
DR EMBL; BC000167; AAH00167.1; -; mRNA.
DR EMBL; BC009348; AAH09348.1; -; mRNA.
DR CCDS; CCDS10872.1; -. [Q969X6-1]
DR RefSeq; NP_116219.2; NM_032830.2. [Q969X6-1]
DR PDB; 7MQ8; EM; 3.60 A; LN=1-686.
DR PDB; 7MQ9; EM; 3.87 A; LN=1-686.
DR PDB; 7MQA; EM; 2.70 A; LN=1-686.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q969X6; -.
DR SMR; Q969X6; -.
DR BioGRID; 124353; 166.
DR IntAct; Q969X6; 36.
DR MINT; Q969X6; -.
DR STRING; 9606.ENSP00000327179; -.
DR GlyGen; Q969X6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969X6; -.
DR PhosphoSitePlus; Q969X6; -.
DR SwissPalm; Q969X6; -.
DR BioMuta; UTP4; -.
DR DMDM; 41016916; -.
DR SWISS-2DPAGE; Q969X6; -.
DR EPD; Q969X6; -.
DR jPOST; Q969X6; -.
DR MassIVE; Q969X6; -.
DR MaxQB; Q969X6; -.
DR PaxDb; Q969X6; -.
DR PeptideAtlas; Q969X6; -.
DR PRIDE; Q969X6; -.
DR ProteomicsDB; 75873; -. [Q969X6-1]
DR ProteomicsDB; 75874; -. [Q969X6-2]
DR ProteomicsDB; 75875; -. [Q969X6-3]
DR Antibodypedia; 29826; 123 antibodies from 21 providers.
DR DNASU; 84916; -.
DR Ensembl; ENST00000314423.12; ENSP00000327179.7; ENSG00000141076.18. [Q969X6-1]
DR Ensembl; ENST00000352319.8; ENSP00000339164.4; ENSG00000141076.18. [Q969X6-2]
DR Ensembl; ENST00000563094.5; ENSP00000456622.1; ENSG00000141076.18. [Q969X6-3]
DR Ensembl; ENST00000575702.3; ENSP00000458843.2; ENSG00000262788.3.
DR GeneID; 84916; -.
DR KEGG; hsa:84916; -.
DR MANE-Select; ENST00000314423.12; ENSP00000327179.7; NM_032830.3; NP_116219.2.
DR UCSC; uc002ewr.3; human. [Q969X6-1]
DR CTD; 84916; -.
DR DisGeNET; 84916; -.
DR GeneCards; UTP4; -.
DR HGNC; HGNC:1983; UTP4.
DR HPA; ENSG00000141076; Low tissue specificity.
DR MalaCards; UTP4; -.
DR MIM; 607456; gene.
DR neXtProt; NX_Q969X6; -.
DR OpenTargets; ENSG00000141076; -.
DR Orphanet; 168583; Hereditary North American Indian childhood cirrhosis.
DR PharmGKB; PA26520; -.
DR VEuPathDB; HostDB:ENSG00000141076; -.
DR eggNOG; KOG2048; Eukaryota.
DR GeneTree; ENSGT00940000153533; -.
DR HOGENOM; CLU_002392_3_0_1; -.
DR InParanoid; Q969X6; -.
DR OMA; PDANWIC; -.
DR OrthoDB; 376282at2759; -.
DR PhylomeDB; Q969X6; -.
DR TreeFam; TF313159; -.
DR PathwayCommons; Q969X6; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q969X6; -.
DR BioGRID-ORCS; 84916; 741 hits in 1073 CRISPR screens.
DR ChiTaRS; UTP4; human.
DR GeneWiki; CIRH1A; -.
DR GenomeRNAi; 84916; -.
DR Pharos; Q969X6; Tbio.
DR PRO; PR:Q969X6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q969X6; protein.
DR Bgee; ENSG00000141076; Expressed in gastrocnemius and 102 other tissues.
DR ExpressionAtlas; Q969X6; baseline and differential.
DR Genevisible; Q969X6; HS.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0034455; C:t-UTP complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR046351; UTP4.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44163; PTHR44163; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Disease variant;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; rRNA processing; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..686
FT /note="U3 small nucleolar RNA-associated protein 4 homolog"
FT /id="PRO_0000050908"
FT REPEAT 7..50
FT /note="WD 1"
FT REPEAT 51..92
FT /note="WD 2"
FT REPEAT 93..135
FT /note="WD 3"
FT REPEAT 136..181
FT /note="WD 4"
FT REPEAT 182..226
FT /note="WD 5"
FT REPEAT 227..275
FT /note="WD 6"
FT REPEAT 276..317
FT /note="WD 7"
FT REPEAT 318..377
FT /note="WD 8"
FT REPEAT 378..427
FT /note="WD 9"
FT REPEAT 428..475
FT /note="WD 10"
FT REPEAT 476..516
FT /note="WD 11"
FT REPEAT 517..566
FT /note="WD 12"
FT REPEAT 567..627
FT /note="WD 13"
FT REPEAT 628..666
FT /note="WD 14"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 368..482
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009201"
FT VAR_SEQ 612..625
FT /note="PLPNDKTLLYNPFP -> VSSSLLPPKSSSES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11853319,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_009202"
FT VAR_SEQ 626..686
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11853319,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_009203"
FT VARIANT 438
FT /note="R -> H (in dbSNP:rs8056684)"
FT /id="VAR_053388"
FT VARIANT 565
FT /note="R -> W (found in patients with North American Indian
FT childhood cirrhosis; unknown pathological significance;
FT does not affect nucleolar protein location; decreased
FT interaction with HIVEP1 measured in yeast two-hybrid
FT screening; dbSNP:rs119465999)"
FT /evidence="ECO:0000269|PubMed:12417987,
FT ECO:0000269|PubMed:16225863, ECO:0000269|PubMed:19732766"
FT /id="VAR_017445"
FT CONFLICT 101
FT /note="G -> V (in Ref. 2; BAB55116)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="V -> M (in Ref. 2; BAB55251)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="N -> S (in Ref. 2; BAB55100)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="N -> S (in Ref. 2; BAC11214)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="M -> V (in Ref. 2; BAB55100)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="F -> L (in Ref. 2; BAC11214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 76890 MW; 595D8B2F47C03299 CRC64;
MGEFKVHRVR FFNYVPSGIR CVAYNNQSNR LAVSRTDGTV EIYNLSANYF QEKFFPGHES
RATEALCWAE GQRLFSAGLN GEIMEYDLQA LNIKYAMDAF GGPIWSMAAS PSGSQLLVGC
EDGSVKLFQI TPDKIQFERN FDRQKSRILS LSWHPSGTHI AAGSIDYISV FDVKSGSAVH
KMIVDRQYMG VSKRKCIVWG VAFLSDGTII SVDSAGKVQF WDSATGTLVK SHLIANADVQ
SIAVADQEDS FVVGTAEGTV FHFQLVPVTS NSSEKQWVRT KPFQHHTHDV RTVAHSPTAL
ISGGTDTHLV FRPLMEKVEV KNYDAALRKI TFPHRCLISC SKKRQLLLFQ FAHHLELWRL
GSTVATGKNG DTLPLSKNAD HLLHLKTKGP ENIICSCISP CGSWIAYSTV SRFFLYRLNY
EHDNISLKRV SKMPAFLRSA LQILFSEDST KLFVASNQGA LHIVQLSGGS FKHLHAFQPQ
SGTVEAMCLL AVSPDGNWLA ASGTSAGVHV YNVKQLKLHC TVPAYNFPVT AMAIAPNTNN
LVIAHSDQQV FEYSIPDKQY TDWSRTVQKQ GFHHLWLQRD TPITHISFHP KRPMHILLHD
AYMFCIIDKS LPLPNDKTLL YNPFPPTNES DVIRRRTAHA FKISKIYKPL LFMDLLDERT
LVAVERPLDD IIAQLPPPIK KKKFGT