ZKSC4_HUMAN
ID ZKSC4_HUMAN Reviewed; 545 AA.
AC Q969J2; B2RE32; Q5U7L4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Zinc finger protein with KRAB and SCAN domains 4;
DE AltName: Full=P373c6.1;
DE AltName: Full=Zinc finger protein 307;
DE AltName: Full=Zinc finger protein 427;
GN Name=ZKSCAN4; Synonyms=ZNF307, ZNF427;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal heart;
RX PubMed=17910948; DOI=10.1016/j.bbrc.2007.08.180;
RA Li J., Wang Y., Fan X., Mo X., Wang Z., Li Y., Yin Z., Deng Y., Luo N.,
RA Zhu C., Liu M., Ma Q., Ocorr K., Yuan W., Wu X.;
RT "ZNF307, a novel zinc finger gene suppresses p53 and p21 pathway.";
RL Biochem. Biophys. Res. Commun. 363:895-900(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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., 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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26 AND LYS-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26; LYS-29; LYS-178 AND LYS-222,
RP AND IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: May be involved in the transcriptional activation of MDM2 and
CC EP300 genes. {ECO:0000269|PubMed:17910948}.
CC -!- INTERACTION:
CC Q969J2; Q9NP86: CABP5; NbExp=7; IntAct=EBI-2818641, EBI-10311131;
CC Q969J2; Q9UBH0: IL36RN; NbExp=3; IntAct=EBI-2818641, EBI-465156;
CC Q969J2; Q9BS40: LXN; NbExp=6; IntAct=EBI-2818641, EBI-1044504;
CC Q969J2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2818641, EBI-16439278;
CC Q969J2; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-2818641, EBI-9057006;
CC Q969J2; Q96JS3: PGBD1; NbExp=4; IntAct=EBI-2818641, EBI-10290053;
CC Q969J2; P60900: PSMA6; NbExp=3; IntAct=EBI-2818641, EBI-357793;
CC Q969J2; P57086: SCAND1; NbExp=7; IntAct=EBI-2818641, EBI-745846;
CC Q969J2; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-2818641, EBI-739510;
CC Q969J2; A0A0S2Z6X0: ZKSCAN4; NbExp=3; IntAct=EBI-2818641, EBI-16431094;
CC Q969J2; Q969J2: ZKSCAN4; NbExp=4; IntAct=EBI-2818641, EBI-2818641;
CC Q969J2; Q9P0L1: ZKSCAN7; NbExp=4; IntAct=EBI-2818641, EBI-743851;
CC Q969J2; Q9P0L1-2: ZKSCAN7; NbExp=6; IntAct=EBI-2818641, EBI-10698225;
CC Q969J2; P17028: ZNF24; NbExp=5; IntAct=EBI-2818641, EBI-707773;
CC Q969J2; Q8NF99-2: ZNF397; NbExp=3; IntAct=EBI-2818641, EBI-11524467;
CC Q969J2; Q9NWS9-2: ZNF446; NbExp=9; IntAct=EBI-2818641, EBI-740232;
CC Q969J2; Q96IT1: ZNF496; NbExp=10; IntAct=EBI-2818641, EBI-743906;
CC Q969J2; Q9Y5A6: ZSCAN21; NbExp=4; IntAct=EBI-2818641, EBI-10281938;
CC Q969J2; P10073: ZSCAN22; NbExp=3; IntAct=EBI-2818641, EBI-10178224;
CC Q969J2; Q86W11: ZSCAN30; NbExp=3; IntAct=EBI-2818641, EBI-11793064;
CC Q969J2; Q9NX65: ZSCAN32; NbExp=5; IntAct=EBI-2818641, EBI-739949;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC ECO:0000269|PubMed:17910948}.
CC -!- TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta, lung and
CC kidney, but not in adult liver and skeletal muscle. In 17-day old
CC embryo, detected in liver, skeletal muscle, brain, heart and small
CC intestine. {ECO:0000269|PubMed:17910948}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY781778; AAV41023.1; -; mRNA.
DR EMBL; AK315783; BAG38129.1; -; mRNA.
DR EMBL; AL022393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03142.1; -; Genomic_DNA.
DR EMBL; BC014031; AAH14031.1; -; mRNA.
DR CCDS; CCDS4647.1; -.
DR RefSeq; NP_061983.2; NM_019110.4.
DR RefSeq; XP_005249152.1; XM_005249095.3.
DR AlphaFoldDB; Q969J2; -.
DR SMR; Q969J2; -.
DR BioGRID; 132179; 72.
DR IntAct; Q969J2; 55.
DR MINT; Q969J2; -.
DR STRING; 9606.ENSP00000366509; -.
DR iPTMnet; Q969J2; -.
DR PhosphoSitePlus; Q969J2; -.
DR BioMuta; ZKSCAN4; -.
DR DMDM; 23396993; -.
DR EPD; Q969J2; -.
DR jPOST; Q969J2; -.
DR MassIVE; Q969J2; -.
DR MaxQB; Q969J2; -.
DR PaxDb; Q969J2; -.
DR PeptideAtlas; Q969J2; -.
DR PRIDE; Q969J2; -.
DR ProteomicsDB; 75772; -.
DR ABCD; Q969J2; 1 sequenced antibody.
DR Antibodypedia; 11231; 251 antibodies from 23 providers.
DR DNASU; 387032; -.
DR Ensembl; ENST00000377294.3; ENSP00000366509.2; ENSG00000187626.9.
DR GeneID; 387032; -.
DR KEGG; hsa:387032; -.
DR MANE-Select; ENST00000377294.3; ENSP00000366509.2; NM_019110.5; NP_061983.2.
DR UCSC; uc003nks.2; human.
DR CTD; 387032; -.
DR DisGeNET; 387032; -.
DR GeneCards; ZKSCAN4; -.
DR HGNC; HGNC:13854; ZKSCAN4.
DR HPA; ENSG00000187626; Low tissue specificity.
DR MIM; 611643; gene.
DR neXtProt; NX_Q969J2; -.
DR OpenTargets; ENSG00000187626; -.
DR PharmGKB; PA162409784; -.
DR VEuPathDB; HostDB:ENSG00000187626; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159644; -.
DR HOGENOM; CLU_002678_49_4_1; -.
DR InParanoid; Q969J2; -.
DR OMA; GHCREDA; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q969J2; -.
DR TreeFam; TF350830; -.
DR PathwayCommons; Q969J2; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q969J2; -.
DR BioGRID-ORCS; 387032; 13 hits in 1100 CRISPR screens.
DR GenomeRNAi; 387032; -.
DR Pharos; Q969J2; Tbio.
DR PRO; PR:Q969J2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q969J2; protein.
DR Bgee; ENSG00000187626; Expressed in sperm and 154 other tissues.
DR ExpressionAtlas; Q969J2; baseline and differential.
DR Genevisible; Q969J2; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..545
FT /note="Zinc finger protein with KRAB and SCAN domains 4"
FT /id="PRO_0000047525"
FT DOMAIN 53..135
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 221..317
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 320..342
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..370
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..398
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 33
FT /note="S -> F (in dbSNP:rs9986596)"
FT /id="VAR_059951"
SQ SEQUENCE 545 AA; 61579 MW; CCFB6B5D976926ED CRC64;
MAREPRKNAA LDAQSAEDQT GLLTVKVEKE EASALTAEVR APCSPARGPE RSRQRFRGFR
YPEAAGPREA LSRLRELCGQ WLQPEMHSKE QILELLVLEQ FLTILPGNLQ SWVREQHPES
GEEVVVLLEY LERQLDEPAP QVPVGDQGQE LLCCKMALLT QTQGSQSSQC QPMKALFKHE
SLGSQPLHDR VLQVPGLAQG GCCREDAMVA SRLTPGSQGL LKMEDVALTL TPGWTQLDSS
QVNLYRDEKQ ENHSSLVSLG GEIQTKSRDL PPVKKLPEKE HGKICHLRED IAQIPTHAEA
GEQEGRLQRK QKNAIGSRRH YCHECGKSFA QSSGLTKHRR IHTGEKPYEC EDCGKTFIGS
SALVIHQRVH TGEKPYECEE CGKVFSHSSN LIKHQRTHTG EKPYECDDCG KTFSQSCSLL
EHHKIHTGEK PYQCNMCGKA FRRNSHLLRH QRIHGDKNVQ NPEHGESWES QGRTESQWEN
TEAPVSYKCN ECERSFTRNR SLIEHQKIHT GEKPYQCDTC GKGFTRTSYL VQHQRSHVGK
KTLSQ
