IPO5_MOUSE
ID IPO5_MOUSE Reviewed; 1097 AA.
AC Q8BKC5; Q3TEG2; Q7TQC6; Q9EQ30;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Importin-5;
DE Short=Imp5;
DE AltName: Full=Importin subunit beta-3;
DE AltName: Full=Karyopherin beta-3;
DE AltName: Full=Ran-binding protein 5;
DE Short=RanBP5;
GN Name=Ipo5; Synonyms=Kpnb3, Ranbp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RA Anway M.D., Li Y., Griswold M.D.;
RT "Identification of testicular germ cell gene expression by differential
RT display analysis.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, AND INTERACTION WITH HISTONES H2B; H2A; H3 AND H4.
RX PubMed=11493596; DOI=10.1093/embo-reports/kve168;
RA Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.;
RT "Multiple pathways contribute to nuclear import of core histones.";
RL EMBO Rep. 2:690-696(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17143267; DOI=10.1038/ncb1519;
RA Nakamura T., Arai Y., Umehara H., Masuhara M., Kimura T., Taniguchi H.,
RA Sekimoto T., Ikawa M., Yoneda Y., Okabe M., Tanaka S., Shiota K.,
RA Nakano T.;
RT "PGC7/Stella protects against DNA demethylation in early embryogenesis.";
RL Nat. Cell Biol. 9:64-71(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=22730302; DOI=10.1093/nar/gks598;
RA Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
RT "NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3.";
RL Nucleic Acids Res. 40:8484-8498(2012).
RN [8]
RP REPEAT STRUCTURE.
RX PubMed=23541588; DOI=10.1016/j.jmb.2013.02.035;
RA Kobayashi J., Matsuura Y.;
RT "Structural basis for cell-cycle-dependent nuclear import mediated by the
RT karyopherin Kap121p.";
RL J. Mol. Biol. 425:1852-1868(2013).
RN [9]
RP INTERACTION WITH AIFM2.
RX PubMed=26689472; DOI=10.1016/j.freeradbiomed.2015.12.002;
RA Miriyala S., Thippakorn C., Chaiswing L., Xu Y., Noel T., Tovmasyan A.,
RA Batinic-Haberle I., Vander Kooi C.W., Chi W., Latif A.A., Panchatcharam M.,
RA Prachayasittikul V., Butterfield D.A., Vore M., Moscow J., St Clair D.K.;
RT "Novel role of 4-hydroxy-2-nonenal in AIFm2-mediated mitochondrial stress
RT signaling.";
RL Free Radic. Biol. Med. 91:68-80(2016).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to the importin, the
CC importin/substrate complex dissociates and importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus. Mediates the nuclear import of ribosomal
CC proteins RPL23A, RPS7 and RPL5. In vitro, mediates nuclear import of
CC H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear
CC import following neuronal stimulation (PubMed:22730302).
CC {ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:17143267,
CC ECO:0000269|PubMed:22730302}.
CC -!- SUBUNIT: Interacts with RPS7 and RPL5 (By similarity). Directly
CC interacts with RPL23A (via BIB domain) (By similarity). Interacts with
CC H2A, H2B, H3 and H4 histones (PubMed:11493596). Interacts with CPEB3;
CC this mediates CPEB3 nuclear import following neuronal stimulation which
CC enhances the interaction in a RAN-regulated manner (By similarity).
CC Interacts with AIFM2; this interaction likely mediates the
CC translocation of AIFM2 into the nucleus upon oxidative stress (By
CC similarity). Interacts with STX3 (isoform 3) (PubMed:26689472).
CC Interacts with SRP19 (By similarity). {ECO:0000250|UniProtKB:O00410,
CC ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:26689472}.
CC -!- INTERACTION:
CC Q8BKC5; P70315: Was; NbExp=8; IntAct=EBI-643605, EBI-644195;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17143267}. Nucleus
CC {ECO:0000269|PubMed:17143267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BKC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKC5-2; Sequence=VSP_009658;
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG45965.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF294327; AAG45965.2; ALT_INIT; mRNA.
DR EMBL; AK053681; BAC35471.1; -; mRNA.
DR EMBL; AK169664; BAE41286.1; -; mRNA.
DR EMBL; BC052392; AAH52392.1; -; mRNA.
DR EMBL; BC054814; AAH54814.1; -; mRNA.
DR CCDS; CCDS37014.1; -. [Q8BKC5-1]
DR RefSeq; NP_076068.1; NM_023579.4. [Q8BKC5-1]
DR RefSeq; XP_006519603.1; XM_006519540.2.
DR AlphaFoldDB; Q8BKC5; -.
DR SMR; Q8BKC5; -.
DR BioGRID; 214142; 20.
DR IntAct; Q8BKC5; 4.
DR STRING; 10090.ENSMUSP00000032898; -.
DR iPTMnet; Q8BKC5; -.
DR PhosphoSitePlus; Q8BKC5; -.
DR SwissPalm; Q8BKC5; -.
DR EPD; Q8BKC5; -.
DR jPOST; Q8BKC5; -.
DR MaxQB; Q8BKC5; -.
DR PaxDb; Q8BKC5; -.
DR PeptideAtlas; Q8BKC5; -.
DR PRIDE; Q8BKC5; -.
DR ProteomicsDB; 269082; -. [Q8BKC5-1]
DR ProteomicsDB; 269083; -. [Q8BKC5-2]
DR Antibodypedia; 3967; 187 antibodies from 30 providers.
DR DNASU; 70572; -.
DR Ensembl; ENSMUST00000032898; ENSMUSP00000032898; ENSMUSG00000030662. [Q8BKC5-1]
DR GeneID; 70572; -.
DR KEGG; mmu:70572; -.
DR UCSC; uc007uzz.1; mouse. [Q8BKC5-1]
DR CTD; 3843; -.
DR MGI; MGI:1917822; Ipo5.
DR VEuPathDB; HostDB:ENSMUSG00000030662; -.
DR eggNOG; KOG2171; Eukaryota.
DR GeneTree; ENSGT00940000155502; -.
DR HOGENOM; CLU_003794_0_0_1; -.
DR InParanoid; Q8BKC5; -.
DR OMA; PKRFVQE; -.
DR OrthoDB; 90499at2759; -.
DR PhylomeDB; Q8BKC5; -.
DR TreeFam; TF300344; -.
DR BioGRID-ORCS; 70572; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Ipo5; mouse.
DR PRO; PR:Q8BKC5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BKC5; protein.
DR Bgee; ENSMUSG00000030662; Expressed in seminiferous tubule of testis and 255 other tissues.
DR Genevisible; Q8BKC5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR InterPro; IPR041653; Importin_rep_4.
DR InterPro; IPR040928; Importin_rep_5.
DR InterPro; IPR041389; Importin_rep_6.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF18808; Importin_rep_4; 1.
DR Pfam; PF18816; Importin_rep_5; 1.
DR Pfam; PF18829; Importin_rep_6; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00410"
FT CHAIN 2..1097
FT /note="Importin-5"
FT /id="PRO_0000120772"
FT REPEAT 5..38
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT DOMAIN 28..99
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 43..77
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 95..122
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 130..157
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 167..201
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 210..246
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 254..289
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 298..350
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 352..386
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 390..430
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 432..472
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 475..523
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 525..568
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 570..615
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 617..692
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 695..737
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 741..780
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 787..853
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 856..895
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 903..935
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 943..983
FT /note="HEAT 21"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 990..1021
FT /note="HEAT 22"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 1032..1067
FT /note="HEAT 23"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 1070..1093
FT /note="HEAT 24"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REGION 325..375
FT /note="Ran-GTP binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00410"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009658"
FT CONFLICT 2
FT /note="A -> TA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="L -> V (in Ref. 1; AAG45965)"
FT /evidence="ECO:0000305"
FT CONFLICT 800..801
FT /note="KL -> NV (in Ref. 1; AAG45965)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="Y -> H (in Ref. 3; AAH54814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1097 AA; 123591 MW; B3197CFC72F3377D CRC64;
MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGRS KITFLLQAIR NTTAAEEARQ
MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME TQSSMRKKIC DIAAELARNL
IDEDGNNQWP EGLKFLFDSV SSQNMGLREA ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC
MQDQEHPSIR TLSARATAAF ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL
VEIADTVPKY LRPHLEATLQ LSLKLCGDTN LNNMQRQLAL EVIVTLSETA AAMLRKHTSL
IAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL GGKLVLPMIK
EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI VNFVLLFLQD PHPRVRYAAC
NAVGQMATDF APGFQKKFHE KVIAALLQTM EDQGNQRVQA HAAAALINFT EDCPKSLLIP
YLDNLVKHLH SIMVLKLQEL IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH
IVENAVQKEL RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ
ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN MSDDDGWEFV
NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT EQVVKLMVPL LKFYFHDGVR
VAAAESMPLL LECARVRGPE YLTQMWHFMC DALIKAIGTE PDSDVLSEIM HSFAKCIEVM
GDGCLNNEHF EELGGILKAK LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT
KVSDILHSIF SSYKEKVLPW FEQLLPLIVN LICPQRPWPD RQWGLCIFDD IVEHCSPASF
KYAEYFISPM LQYVCDNSPE VRQAAAYGLG VMAQFGGDNY RPFCTDALPL LVRVIQAPEA
KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL PLHEDKEEAV QTFSYLCDLI
ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA IKHEDPCAKR LANVVRQVQT SGGLWTECIA
QLSPEQQAAI QELLNSA
