INT4_HUMAN
ID INT4_HUMAN Reviewed; 963 AA.
AC Q96HW7; Q2YD62; Q6PJG4; Q7Z4E7; Q96G32; Q96GA1; Q9BRC0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Integrator complex subunit 4;
DE Short=Int4;
GN Name=INTS4; ORFNames=MSTP093;
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] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 174-963 (ISOFORM 1).
RC TISSUE=Brain, Muscle, Ovary, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 641-963 (ISOFORM 1).
RC TISSUE=Aorta;
RA Sheng H., Qin B.M., Liu Y.Q., Zhao B., Liu B., Wang X.Y., Zhang Q.,
RA Song L., Gao Y., Zhang C.L., Ye J., Ji X.J., Liu B.H., Lu H., Xu H.S.,
RA Chen J.Z., Cai M.Q., Zheng W.Y., Teng C.Y., Liu Q., Yu L.T., Lin J.,
RA Gong J., Zhang A.M., Gao R.L., Hui R.T.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE INTEGRATOR COMPLEX.
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [4]
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).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA Reversade B., Wagner E.J., Lee L.A.;
RT "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT its role in the integrator complex.";
RL Mol. Biol. Cell 24:2954-2965(2013).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-791, AND IDENTIFICATION BY MASS
RP 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-791, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-791, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-791, 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).
CC -!- FUNCTION: Component of the Integrator (INT) complex, a complex involved
CC in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their
CC 3'-box-dependent processing. The Integrator complex is associated with
CC the C-terminal domain (CTD) of RNA polymerase II largest subunit
CC (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable).
CC Mediates recruitment of cytoplasmic dynein to the nuclear envelope,
CC probably as component of the INT complex (PubMed:23904267).
CC {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12.
CC {ECO:0000269|PubMed:16239144}.
CC -!- INTERACTION:
CC Q96HW7; O14964: HGS; NbExp=4; IntAct=EBI-5663129, EBI-740220;
CC Q96HW7; Q9NV88: INTS9; NbExp=2; IntAct=EBI-5663129, EBI-2866634;
CC Q96HW7; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-5663129, EBI-739895;
CC Q96HW7; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-5663129, EBI-10182121;
CC Q96HW7-2; O14964: HGS; NbExp=3; IntAct=EBI-16438029, EBI-740220;
CC Q96HW7-3; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-12240836, EBI-12039345;
CC Q96HW7-3; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-12240836, EBI-18582591;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23904267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96HW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HW7-2; Sequence=VSP_021450;
CC Name=3;
CC IsoId=Q96HW7-3; Sequence=VSP_021448, VSP_021449, VSP_021452,
CC VSP_021453;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Integrator subunit 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13616.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; 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; BC006369; AAH06369.1; -; mRNA.
DR EMBL; BC008013; AAH08013.1; -; mRNA.
DR EMBL; BC009859; AAH09859.2; -; mRNA.
DR EMBL; BC009995; AAH09995.1; -; mRNA.
DR EMBL; BC015664; AAH15664.1; -; mRNA.
DR EMBL; AF172822; AAQ13616.1; ALT_SEQ; mRNA.
DR EMBL; BK005723; DAA05723.1; -; mRNA.
DR CCDS; CCDS31644.1; -. [Q96HW7-1]
DR RefSeq; NP_291025.3; NM_033547.3. [Q96HW7-1]
DR PDB; 7BFP; EM; 3.50 A; C=1-963.
DR PDB; 7BFQ; EM; 3.50 A; C=1-963.
DR PDB; 7CUN; EM; 3.50 A; D=1-963.
DR PDB; 7PKS; EM; 3.60 A; d=1-963.
DR PDBsum; 7BFP; -.
DR PDBsum; 7BFQ; -.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q96HW7; -.
DR SMR; Q96HW7; -.
DR BioGRID; 124909; 110.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q96HW7; -.
DR IntAct; Q96HW7; 41.
DR MINT; Q96HW7; -.
DR STRING; 9606.ENSP00000434466; -.
DR iPTMnet; Q96HW7; -.
DR MetOSite; Q96HW7; -.
DR PhosphoSitePlus; Q96HW7; -.
DR SwissPalm; Q96HW7; -.
DR BioMuta; INTS4; -.
DR DMDM; 118572560; -.
DR EPD; Q96HW7; -.
DR jPOST; Q96HW7; -.
DR MassIVE; Q96HW7; -.
DR MaxQB; Q96HW7; -.
DR PaxDb; Q96HW7; -.
DR PeptideAtlas; Q96HW7; -.
DR PRIDE; Q96HW7; -.
DR ProteomicsDB; 76789; -. [Q96HW7-1]
DR ProteomicsDB; 76790; -. [Q96HW7-2]
DR ProteomicsDB; 76791; -. [Q96HW7-3]
DR Antibodypedia; 31280; 132 antibodies from 26 providers.
DR DNASU; 92105; -.
DR Ensembl; ENST00000529807.5; ENSP00000433644.1; ENSG00000149262.17. [Q96HW7-2]
DR Ensembl; ENST00000534064.6; ENSP00000434466.1; ENSG00000149262.17. [Q96HW7-1]
DR GeneID; 92105; -.
DR KEGG; hsa:92105; -.
DR MANE-Select; ENST00000534064.6; ENSP00000434466.1; NM_033547.4; NP_291025.3.
DR UCSC; uc001oys.4; human. [Q96HW7-1]
DR CTD; 92105; -.
DR DisGeNET; 92105; -.
DR GeneCards; INTS4; -.
DR HGNC; HGNC:25048; INTS4.
DR HPA; ENSG00000149262; Low tissue specificity.
DR MIM; 611348; gene.
DR neXtProt; NX_Q96HW7; -.
DR OpenTargets; ENSG00000149262; -.
DR PharmGKB; PA144596421; -.
DR VEuPathDB; HostDB:ENSG00000149262; -.
DR eggNOG; KOG2259; Eukaryota.
DR GeneTree; ENSGT00390000010128; -.
DR HOGENOM; CLU_012910_1_0_1; -.
DR InParanoid; Q96HW7; -.
DR OMA; PHMQGSF; -.
DR OrthoDB; 256550at2759; -.
DR PhylomeDB; Q96HW7; -.
DR TreeFam; TF315047; -.
DR PathwayCommons; Q96HW7; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q96HW7; -.
DR SIGNOR; Q96HW7; -.
DR BioGRID-ORCS; 92105; 735 hits in 1093 CRISPR screens.
DR ChiTaRS; INTS4; human.
DR GenomeRNAi; 92105; -.
DR Pharos; Q96HW7; Tdark.
DR PRO; PR:Q96HW7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96HW7; protein.
DR Bgee; ENSG00000149262; Expressed in buccal mucosa cell and 178 other tissues.
DR ExpressionAtlas; Q96HW7; baseline and differential.
DR Genevisible; Q96HW7; HS.
DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..963
FT /note="Integrator complex subunit 4"
FT /id="PRO_0000259538"
FT REPEAT 66..105
FT /note="HEAT 1"
FT REPEAT 145..183
FT /note="HEAT 2"
FT REPEAT 190..228
FT /note="HEAT 3"
FT REPEAT 229..263
FT /note="HEAT 4"
FT REPEAT 277..313
FT /note="HEAT 5"
FT REPEAT 369..405
FT /note="HEAT 6"
FT REPEAT 406..444
FT /note="HEAT 7"
FT REPEAT 446..484
FT /note="HEAT 8"
FT MOD_RES 26
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CIM8"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021448"
FT VAR_SEQ 149..156
FT /note="MRLVDVAC -> MPSTSCRM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021449"
FT VAR_SEQ 506..963
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021450"
FT VAR_SEQ 642..659
FT /note="DLQRLGELQSELAGVADF -> VEVSPWWPGWSQTPELK (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021452"
FT VAR_SEQ 660..963
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021453"
FT CONFLICT 900..901
FT /note="HT -> PP (in Ref. 2; AAQ13616)"
FT /evidence="ECO:0000305"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:7BFP"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:7BFP"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 388..404
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 479..495
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 516..521
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 568..579
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 629..649
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 654..674
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 677..680
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 692..695
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 696..709
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 716..740
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 744..764
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 767..771
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 776..787
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 792..803
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 845..847
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:7CUN"
FT TURN 858..860
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 861..866
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 868..870
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 872..875
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 881..886
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 889..892
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 895..897
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 910..915
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 918..920
FT /evidence="ECO:0007829|PDB:7CUN"
SQ SEQUENCE 963 AA; 108171 MW; D56D6480EFC962D7 CRC64;
MAAHLKKRVY EEFTKVVQPQ EEIATKKLRL TKPSKSAALH IDLCKATSPA DALQYLLQFA
RKPVEAESVE GVVRILLEHY YKENDPSVRL KIASLLGLLS KTAGFSPDCI MDDAINILQN
EKSHQVLAQL LDTLLAIGTK LPENQAIQMR LVDVACKHLT DTSHGVRNKC LQLLGNLGSL
EKSVTKDAEG LAARDVQKII GDYFSDQDPR VRTAAIKAML QLHERGLKLH QTIYNQACKL
LSDDYEQVRS AAVQLIWVVS QLYPESIVPI PSSNEEIRLV DDAFGKICHM VSDGSWVVRV
QAAKLLGSME QVSSHFLEQT LDKKLMSDLR RKRTAHERAK ELYSSGEFSS GRKWGDDAPK
EEVDTGAVNL IESGACGAFV HGLEDEMYEV RIAAVEALCM LAQSSPSFAE KCLDFLVDMF
NDEIEEVRLQ SIHTMRKISN NITLREDQLD TVLAVLEDSS RDIREALHEL LCCTNVSTKE
GIHLALVELL KNLTKYPTDR DSIWKCLKFL GSRHPTLVLP LVPELLSTHP FFDTAEPDMD
DPAYIAVLVL IFNAAKTCPT MPALFSDHTF RHYAYLRDSL SHLVPALRLP GRKLVSSAVS
PSIIPQEDPS QQFLQQSLER VYSLQHLDPQ GAQELLEFTI RDLQRLGELQ SELAGVADFS
ATYLRCQLLL IKALQEKLWN VAAPLYLKQS DLASAAAKQI MEETYKMEFM YSGVENKQVV
IIHHMRLQAK ALQLIVTART TRGLDPLFGM CEKFLQEVDF FQRYFIADLP HLQDSFVDKL
LDLMPRLMTS KPAEVVKILQ TMLRQSAFLH LPLPEQIHKA SATIIEPAGE SDNPLRFTSG
LVVALDVDAT LEHVQDPQNT VKVQVLYPDG QAQMIHPKPA DFRNPGPGRH RLITQVYLSH
TAWTEACQVE VRLLLAYNSS ARIPKCPWME GGEMSPQVET SIEGTIPFSK PVKVYIMPKP
ARR
