XPO4_HUMAN
ID XPO4_HUMAN Reviewed; 1151 AA.
AC Q9C0E2; Q5VUZ5; Q8N3V6; Q9H934;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Exportin-4 {ECO:0000303|PubMed:10944119};
DE Short=Exp4 {ECO:0000303|PubMed:10944119};
GN Name=XPO4 {ECO:0000303|PubMed:26787900, ECO:0000312|HGNC:HGNC:17796};
GN Synonyms=KIAA1721 {ECO:0000303|PubMed:11214970};
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].
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1151.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-1151.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION IN NUCLEAR PROTEIN EXPORT, AND
RP IDENTIFICATION IN A COMPLEX WITH RAN AND EIF5A.
RX PubMed=10944119; DOI=10.1093/emboj/19.16.4362;
RA Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S.,
RA Hartmann E., Kutay U., Goerlich D.;
RT "Exportin 4: a mediator of a novel nuclear export pathway in higher
RT eukaryotes.";
RL EMBO J. 19:4362-4371(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN
RP AND SMAD3, INTERACTION WITH SMAD3, AND SUBCELLULAR LOCATION.
RX PubMed=16449645; DOI=10.1128/mcb.26.4.1318-1332.2006;
RA Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y., Heldin C.-H.,
RA Moustakas A.;
RT "The mechanism of nuclear export of Smad3 involves exportin 4 and Ran.";
RL Mol. Cell. Biol. 26:1318-1332(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP FUNCTION.
RX PubMed=26787900; DOI=10.1073/pnas.1520045113;
RA Bhardwaj A., Das S.;
RT "SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic
RT functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E538-E547(2016).
CC -!- FUNCTION: Mediates the nuclear export of proteins (cargos), such as
CC EIF5A, SMAD3 and isoform M2 of PKM (PKM2) (PubMed:10944119,
CC PubMed:16449645, PubMed:26787900). In the nucleus binds cooperatively
CC to its cargo and to the GTPase Ran in its active GTP-bound form.
CC Docking of this trimeric complex to the nuclear pore complex (NPC) is
CC mediated through binding to nucleoporins (PubMed:10944119,
CC PubMed:16449645). Upon transit of a nuclear export complex into the
CC cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to
CC Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of
CC the cargo from the export receptor (PubMed:10944119, PubMed:16449645).
CC XPO4 then return to the nuclear compartment and mediate another round
CC of transport (PubMed:10944119, PubMed:16449645). The directionality of
CC nuclear export is thought to be conferred by an asymmetric distribution
CC of the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (PubMed:10944119, PubMed:16449645). Catalyzes the nuclear
CC export of hypusinated EIF5A; a small cytoplasmic protein that enters
CC nucleus and accumulates within nucleolus if not exported back by XPO4
CC (PubMed:10944119). Specifically mediates nuclear export of isoform M2
CC of PKM (PKM2) following PKM2 deacetylation by SIRT6 (PubMed:26787900).
CC Also mediates the nuclear import of SOX transcription factors SRY and
CC SOX2 (By similarity). {ECO:0000250|UniProtKB:Q9ESJ0,
CC ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:16449645,
CC ECO:0000269|PubMed:26787900}.
CC -!- SUBUNIT: Interacts with Ran and cargo proteins in a GTP-dependent
CC manner. {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:16449645}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16449645}. Nucleus
CC {ECO:0000269|PubMed:16449645}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000269|PubMed:16449645}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB051508; BAB21812.1; -; mRNA.
DR EMBL; AL512652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK023108; BAB14409.1; ALT_INIT; mRNA.
DR EMBL; AL831819; CAD38533.2; -; mRNA.
DR CCDS; CCDS41872.1; -.
DR RefSeq; NP_071904.4; NM_022459.4.
DR AlphaFoldDB; Q9C0E2; -.
DR SMR; Q9C0E2; -.
DR BioGRID; 122138; 102.
DR IntAct; Q9C0E2; 34.
DR MINT; Q9C0E2; -.
DR STRING; 9606.ENSP00000255305; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9C0E2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9C0E2; -.
DR MetOSite; Q9C0E2; -.
DR PhosphoSitePlus; Q9C0E2; -.
DR BioMuta; XPO4; -.
DR DMDM; 17368720; -.
DR EPD; Q9C0E2; -.
DR jPOST; Q9C0E2; -.
DR MassIVE; Q9C0E2; -.
DR MaxQB; Q9C0E2; -.
DR PaxDb; Q9C0E2; -.
DR PeptideAtlas; Q9C0E2; -.
DR PRIDE; Q9C0E2; -.
DR ProteomicsDB; 80019; -.
DR ABCD; Q9C0E2; 1 sequenced antibody.
DR Antibodypedia; 41969; 50 antibodies from 20 providers.
DR DNASU; 64328; -.
DR Ensembl; ENST00000255305.11; ENSP00000255305.6; ENSG00000132953.18.
DR GeneID; 64328; -.
DR KEGG; hsa:64328; -.
DR MANE-Select; ENST00000255305.11; ENSP00000255305.6; NM_022459.5; NP_071904.4.
DR UCSC; uc001unq.5; human.
DR CTD; 64328; -.
DR DisGeNET; 64328; -.
DR GeneCards; XPO4; -.
DR HGNC; HGNC:17796; XPO4.
DR HPA; ENSG00000132953; Tissue enhanced (skeletal).
DR MIM; 611449; gene.
DR neXtProt; NX_Q9C0E2; -.
DR OpenTargets; ENSG00000132953; -.
DR PharmGKB; PA134866468; -.
DR VEuPathDB; HostDB:ENSG00000132953; -.
DR eggNOG; KOG4541; Eukaryota.
DR GeneTree; ENSGT00940000153139; -.
DR HOGENOM; CLU_005818_0_0_1; -.
DR InParanoid; Q9C0E2; -.
DR OMA; KSISCKS; -.
DR OrthoDB; 106880at2759; -.
DR PhylomeDB; Q9C0E2; -.
DR TreeFam; TF312991; -.
DR PathwayCommons; Q9C0E2; -.
DR SignaLink; Q9C0E2; -.
DR BioGRID-ORCS; 64328; 22 hits in 1086 CRISPR screens.
DR ChiTaRS; XPO4; human.
DR GeneWiki; XPO4; -.
DR GenomeRNAi; 64328; -.
DR Pharos; Q9C0E2; Tbio.
DR PRO; PR:Q9C0E2; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9C0E2; protein.
DR Bgee; ENSG00000132953; Expressed in skeletal muscle tissue of rectus abdominis and 150 other tissues.
DR Genevisible; Q9C0E2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR044189; XPO4/7-like.
DR PANTHER; PTHR12596; PTHR12596; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1151
FT /note="Exportin-4"
FT /id="PRO_0000204711"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 149
FT /note="N -> S (in dbSNP:rs17320607)"
FT /id="VAR_048958"
FT VARIANT 451
FT /note="T -> A (in dbSNP:rs9552285)"
FT /id="VAR_048959"
FT CONFLICT 511
FT /note="L -> S (in Ref. 3; BAB14409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1151 AA; 130139 MW; 38E7EEFC938B07C5 CRC64;
MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP FAVCKHILET
SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY VLQRPNLQKY VREQILLAVA
VIVKRGSLDK SIDCKSIFHE VSQLISSGNP TVQTLACSIL TALLSEFSSS SKTSNIGLSM
EFHGNCKRVF QEEDLRQIFM LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP
PNLGRHYIAM FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA
QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN LITVFPRNVL
TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM EAYDKLLESW LTLVQDDKHF
HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL TANGVASREE EEISELQEDD RDQFSDQLAS
VGMLGRIAAE HCIPLLTSLL EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH
WLILVTGYLL ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR
TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL LVDEKLYDQI
SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA NDTVQLLVTL VERRERANLV
IQCENWWNLA KQFASRSPPL NFLSSPVQRT LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ
QRFLRVINQE NFQQMCQQEE VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG
LMEVYKNTPE TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID
VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS AADVVLYGVN
LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE DLFKSLMYSL ELGMTSMSSE
VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT
LVCLHQAEYS ELVETLLSSQ QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF
MANVGGLLCV K
