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Protein Hook homolog 3 (h-hook3) (hHK3)

 HOOK3_HUMAN             Reviewed;         718 AA.
Q86VS8; D3DSY8; Q8NBH0; Q9BY13;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
02-FEB-2004, sequence version 2.
25-OCT-2017, entry version 133.
RecName: Full=Protein Hook homolog 3;
Short=h-hook3;
Short=hHK3;
Name=HOOK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES,
AND SUBCELLULAR LOCATION.
PubMed=11238449; DOI=10.1083/jcb.152.5.923;
Walenta J.H., Didier A.J., Liu X., Kraemer H.;
"The Golgi-associated hook3 protein is a member of a novel family of
microtubule-binding proteins.";
J. Cell Biol. 152:923-934(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-718.
TISSUE=Astrocyte;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
FUNCTION, AND INTERACTION WITH MSR1.
PubMed=17237231; DOI=10.1074/jbc.M611537200;
Sano H., Ishino M., Kraemer H., Shimizu T., Mitsuzawa H.,
Nishitani C., Kuroki Y.;
"The microtubule-binding protein Hook3 interacts with a cytoplasmic
domain of scavenger receptor A.";
J. Biol. Chem. 282:7973-7981(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF
COMPLEX, FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH AKTIP;
HOOK1; HOOK2; VPS16 AND VPS41.
PubMed=18799622; DOI=10.1091/mbc.E08-05-0473;
Xu L., Sowa M.E., Chen J., Li X., Gygi S.P., Harper J.W.;
"An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal
clustering by the homotypic vacuolar protein sorting complex.";
Mol. Biol. Cell 19:5059-5071(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-6; SER-238;
SER-693 AND SER-707, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
FUNCTION, AND INTERACTION WITH DYNEIN INTERMEDIATE CHAIN AND DCTN1.
PubMed=25035494; DOI=10.1126/science.1254198;
McKenney R.J., Huynh W., Tanenbaum M.E., Bhabha G., Vale R.D.;
"Activation of cytoplasmic dynein motility by dynactin-cargo adapter
complexes.";
Science 345:337-341(2014).
[16]
VARIANT [LARGE SCALE ANALYSIS] ARG-221.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Probably serves as a target for the spiC protein from
Salmonella typhimurium, which inactivates it, leading to a strong
alteration in cellular trafficking (By similarity). Component of
the FTS/Hook/FHIP complex (FHF complex). The FHF complex may
function to promote vesicle trafficking and/or fusion via the
homotypic vesicular protein sorting complex (the HOPS complex).
May regulate clearance of endocytosed receptors such as MSR1.
Participates in defining the architecture and localization of the
Golgi complex. Acts as an adapter protein linking the dynein motor
complex to various cargos and converts dynein from a non-
processive to a highly processive motor in the presence of
dynactin. Facilitates the interaction between dynein and dynactin
and activates dynein processivity (the ability to move along a
microtubule for a long distance without falling off the track)
(PubMed:25035494). {ECO:0000250|UniProtKB:Q8BUK6,
ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:17237231,
ECO:0000269|PubMed:18799622, ECO:0000269|PubMed:25035494}.
-!- SUBUNIT: Interacts with Salmonella typhimurium spiC (By
similarity). Self-associates. Component of the FTS/Hook/FHIP
complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or
more members of the Hook family of proteins HOOK1, HOOK2, and
HOOK3. May interact directly with AKTIP/FTS, HOOK1 and HOOK2.
Associates with several subunits of the homotypic vesicular
sorting complex (the HOPS complex) including VPS16 and VPS41;
these interactions may be indirect (PubMed:18799622). Interacts
with MSR1, and this association is stimulated by ligand binding to
MSR1 (PubMed:17237231). Interacts with microtubules
(PubMed:11238449). Interacts with dynein intermediate chain and
dynactin (DCTN1) (PubMed:25035494). Interacts with CCDC181 (By
similarity). Interacts with LRGUK (By similarity).
{ECO:0000250|UniProtKB:Q8BUK6, ECO:0000269|PubMed:11238449,
ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:18799622,
ECO:0000269|PubMed:25035494}.
-!- INTERACTION:
P50222:MEOX2; NbExp=4; IntAct=EBI-1777078, EBI-748397;
P21757:MSR1; NbExp=4; IntAct=EBI-1777078, EBI-1776976;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11238449}. Golgi apparatus
{ECO:0000269|PubMed:11238449}. Note=Enriched at the cis-face of
the Golgi complex. Localizes to microtubule asters in prophase
(PubMed:11238449). Localizes to the manchette in elongating
spermatids (By similarity). {ECO:0000250|UniProtKB:Q8BUK6,
ECO:0000269|PubMed:11238449}.
-!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH48304.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF241830; AAK29204.1; -; mRNA.
EMBL; CH471080; EAW63197.1; -; Genomic_DNA.
EMBL; CH471080; EAW63198.1; -; Genomic_DNA.
EMBL; BC048304; AAH48304.1; ALT_SEQ; mRNA.
EMBL; BC056146; AAH56146.1; -; mRNA.
EMBL; AK090540; BAC03473.1; -; mRNA.
CCDS; CCDS6139.1; -.
RefSeq; NP_115786.1; NM_032410.3.
UniGene; Hs.162852; -.
PDB; 5J8E; X-ray; 1.70 A; A/B=1-160.
PDBsum; 5J8E; -.
ProteinModelPortal; Q86VS8; -.
SMR; Q86VS8; -.
BioGrid; 124068; 37.
CORUM; Q86VS8; -.
IntAct; Q86VS8; 15.
STRING; 9606.ENSP00000305699; -.
iPTMnet; Q86VS8; -.
PhosphoSitePlus; Q86VS8; -.
BioMuta; HOOK3; -.
DMDM; 41688581; -.
EPD; Q86VS8; -.
MaxQB; Q86VS8; -.
PaxDb; Q86VS8; -.
PeptideAtlas; Q86VS8; -.
PRIDE; Q86VS8; -.
Ensembl; ENST00000307602; ENSP00000305699; ENSG00000168172.
GeneID; 84376; -.
KEGG; hsa:84376; -.
UCSC; uc003xpr.4; human.
CTD; 84376; -.
DisGeNET; 84376; -.
EuPathDB; HostDB:ENSG00000168172.8; -.
GeneCards; HOOK3; -.
HGNC; HGNC:23576; HOOK3.
HPA; HPA024756; -.
MIM; 607825; gene.
neXtProt; NX_Q86VS8; -.
OpenTargets; ENSG00000168172; -.
PharmGKB; PA134961305; -.
eggNOG; ENOG410IG1M; Eukaryota.
eggNOG; ENOG410XQ3G; LUCA.
GeneTree; ENSGT00690000101702; -.
HOGENOM; HOG000294112; -.
HOVERGEN; HBG051920; -.
InParanoid; Q86VS8; -.
KO; K16536; -.
OMA; DELKCGQ; -.
OrthoDB; EOG091G06O9; -.
PhylomeDB; Q86VS8; -.
TreeFam; TF320231; -.
SIGNOR; Q86VS8; -.
ChiTaRS; HOOK3; human.
GeneWiki; HOOK3; -.
GenomeRNAi; 84376; -.
PRO; PR:Q86VS8; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000168172; -.
CleanEx; HS_HOOK3; -.
ExpressionAtlas; Q86VS8; baseline and differential.
Genevisible; Q86VS8; HS.
GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
GO; GO:0005813; C:centrosome; ISS:BHF-UCL.
GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0070695; C:FHF complex; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0000242; C:pericentriolar material; ISS:BHF-UCL.
GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
GO; GO:0051645; P:Golgi localization; IMP:UniProtKB.
GO; GO:0022027; P:interkinetic nuclear migration; ISS:BHF-UCL.
GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:BHF-UCL.
GO; GO:0050768; P:negative regulation of neurogenesis; ISS:BHF-UCL.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0071539; P:protein localization to centrosome; ISS:BHF-UCL.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR008636; Hook-like_fam.
PANTHER; PTHR18947; PTHR18947; 1.
Pfam; PF05622; HOOK; 1.
PROSITE; PS50021; CH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Transport.
CHAIN 1 718 Protein Hook homolog 3.
/FTId=PRO_0000219197.
DOMAIN 10 126 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REGION 1 164 Sufficient for interaction with
microtubules.
REGION 553 718 Required for association with Golgi.
REGION 556 718 Required for interaction with MSR1.
{ECO:0000269|PubMed:17237231}.
COILED 167 433 {ECO:0000255}.
COILED 462 667 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 693 693 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 221 221 Q -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035710.
VARIANT 670 670 Y -> S (in dbSNP:rs34131505).
/FTId=VAR_049363.
CONFLICT 348 348 M -> V (in Ref. 4; BAC03473).
{ECO:0000305}.
HELIX 10 20 {ECO:0000244|PDB:5J8E}.
HELIX 21 23 {ECO:0000244|PDB:5J8E}.
HELIX 32 35 {ECO:0000244|PDB:5J8E}.
HELIX 39 48 {ECO:0000244|PDB:5J8E}.
TURN 50 52 {ECO:0000244|PDB:5J8E}.
HELIX 55 58 {ECO:0000244|PDB:5J8E}.
HELIX 69 89 {ECO:0000244|PDB:5J8E}.
HELIX 103 109 {ECO:0000244|PDB:5J8E}.
HELIX 112 128 {ECO:0000244|PDB:5J8E}.
HELIX 132 157 {ECO:0000244|PDB:5J8E}.
SEQUENCE 718 AA; 83126 MW; 9528EC9C854D39FA CRC64;
MFSVESLERA ELCESLLTWI QTFNVDAPCQ TVEDLTNGVV MAQVLQKIDP AYFDENWLNR
IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL PDVNLIGEHS DAAELGRMLQ
LILGCAVNCE QKQEYIQAIM MMEESVQHVV MTAIQELMSK ESPVSAGNDA YVDLDRQLKK
TTEELNEALS AKEEIAQRCH ELDMQVAALQ EEKSSLLAEN QVLMERLNQS DSIEDPNSPA
GRRHLQLQTQ LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK
DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN TVSLEEELRK
ANAARSQLET YKRQVVELQN RLSEESKKAD KLDFEYKRLK EKVDSLQKEK DRLRTERDSL
KETIEELRCV QAQEGQLTTQ GLMPLGSQES SDSLAAEIVT PEIREKLIRL QHENKMLKLN
QEGSDNEKIA LLQSLLDDAN LRKNELETEN RLVNQRLLEV QSQVEELQKS LQDQGSKAED
SVLLKKKLEE HLEKLHEANN ELQKKRAIIE DLEPRFNNSS LKIEELQEAL RKKEEEMKQM
EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE YEKTKSQREM
EEKYIVSAWY NMGMTLHKKA AEDRLASTGS GQSFLARQRQ ATSSRRSYPG HVQPATAR


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