PO210_MOUSE
ID PO210_MOUSE Reviewed; 1886 AA.
AC Q9QY81; Q3U031; Q69ZW2; Q7TQM1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear pore membrane glycoprotein 210;
DE Short=Nuclear pore protein gp210;
DE AltName: Full=Nuclear envelope pore membrane protein POM 210;
DE Short=POM210;
DE AltName: Full=Nucleoporin Nup210;
DE AltName: Full=Pore membrane protein of 210 kDa;
DE Flags: Precursor;
GN Name=Nup210; Synonyms=Kiaa0906;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=NMRI; TISSUE=Kidney;
RX PubMed=10469352; DOI=10.1046/j.1523-1755.1999.00618.x;
RA Olsson M., Ekblom M., Fecker L., Kurkinen M., Ekblom P.;
RT "cDNA cloning and embryonic expression of mouse nuclear pore membrane
RT glycoprotein 210 mRNA.";
RL Kidney Int. 56:827-838(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1886.
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1160.
RC TISSUE=Spleen;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1839; THR-1844 AND SER-1873,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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).
CC -!- FUNCTION: Nucleoporin essential for nuclear pore assembly and fusion,
CC nuclear pore spacing, as well as structural integrity.
CC -!- SUBUNIT: Forms dimers and possibly higher-order oligomers.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}.
CC Nucleus membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Preferential expressed in epithelial cells. In the
CC kidney, expression was seen in both the epithelium derived from the
CC ureteric tree and the mesenchyme-derived epithelium. In other tissues
CC of 13-day-old embryos, expression was also confined to the epithelium.
CC In nervous tissues, mainly expressed in the olfactory epithelium and
CC walls of the lateral ventricle. Weak expression was seen in the heart.
CC {ECO:0000269|PubMed:10469352}.
CC -!- PTM: N-glycosylated, but not all potential glycosylation sites may be
CC used. Contains high-mannose type oligosaccharides (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-1880 in mitosis specifically; not
CC phosphorylated in interphase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NUP210 family. {ECO:0000305}.
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DR EMBL; AF113751; AAF21969.1; -; mRNA.
DR EMBL; BC052468; AAH52468.1; -; mRNA.
DR EMBL; AK173056; BAD32334.1; -; mRNA.
DR EMBL; AK157272; BAE34024.1; -; mRNA.
DR CCDS; CCDS39565.1; -.
DR RefSeq; NP_061285.2; NM_018815.2.
DR AlphaFoldDB; Q9QY81; -.
DR BioGRID; 207678; 2.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q9QY81; 1.
DR STRING; 10090.ENSMUSP00000032179; -.
DR GlyConnect; 2567; 5 N-Linked glycans (4 sites).
DR GlyGen; Q9QY81; 12 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q9QY81; -.
DR PhosphoSitePlus; Q9QY81; -.
DR SwissPalm; Q9QY81; -.
DR EPD; Q9QY81; -.
DR jPOST; Q9QY81; -.
DR MaxQB; Q9QY81; -.
DR PaxDb; Q9QY81; -.
DR PeptideAtlas; Q9QY81; -.
DR PRIDE; Q9QY81; -.
DR ProteomicsDB; 289353; -.
DR Antibodypedia; 10858; 207 antibodies from 26 providers.
DR DNASU; 54563; -.
DR Ensembl; ENSMUST00000032179; ENSMUSP00000032179; ENSMUSG00000030091.
DR GeneID; 54563; -.
DR KEGG; mmu:54563; -.
DR UCSC; uc009cxu.2; mouse.
DR CTD; 23225; -.
DR MGI; MGI:1859555; Nup210.
DR VEuPathDB; HostDB:ENSMUSG00000030091; -.
DR eggNOG; KOG1833; Eukaryota.
DR GeneTree; ENSGT00390000009491; -.
DR HOGENOM; CLU_001205_1_1_1; -.
DR InParanoid; Q9QY81; -.
DR OMA; AELHIRE; -.
DR OrthoDB; 843414at2759; -.
DR PhylomeDB; Q9QY81; -.
DR TreeFam; TF313331; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 54563; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Nup210; mouse.
DR PRO; PR:Q9QY81; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QY81; protein.
DR Bgee; ENSMUSG00000030091; Expressed in peripheral lymph node and 236 other tissues.
DR ExpressionAtlas; Q9QY81; baseline and differential.
DR Genevisible; Q9QY81; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR045197; NUP210-like.
DR PANTHER; PTHR23019; PTHR23019; 1.
DR Pfam; PF02368; Big_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Signal; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..1886
FT /note="Nuclear pore membrane glycoprotein 210"
FT /id="PRO_0000236047"
FT TOPO_DOM 27..1808
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 1809..1829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1830..1886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 1078..1151
FT /note="BIG2"
FT /evidence="ECO:0000255"
FT MOD_RES 1839
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1844
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT MOD_RES 1880
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT MOD_RES 1885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEM1"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="L -> V (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="F -> G (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="LR -> VA (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="A -> S (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="L -> F (in Ref. 4; BAE34024)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..513
FT /note="SV -> RE (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..518
FT /note="HD -> QH (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="R -> K (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 719..762
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="Q -> E (in Ref. 4; BAE34024)"
FT /evidence="ECO:0000305"
FT CONFLICT 812..814
FT /note="SRP -> FPR (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="I -> V (in Ref. 4; BAE34024)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="A -> T (in Ref. 4; BAE34024)"
FT /evidence="ECO:0000305"
FT CONFLICT 974..975
FT /note="HV -> QL (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020..1021
FT /note="KL -> NW (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 1049
FT /note="V -> C (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="V -> L (in Ref. 1; AAF21969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1886 AA; 204101 MW; 8732FBAA46096862 CRC64;
MARASLVQPA LWALLLLQVV GPAAAAKLNI PKVLLPFTRA TRVNFTLEAS EGCYRWSSTR
PEVASIEPLG SSEQQCSQKA VVQARLTQPA RLTSIIFAED ITTGQVLRCD AIVDLIHGIQ
IVSTTRELYL EDSPLELKIQ ALDSEGNTFS TLAGLVFDWT IVKDTEANGF SDSHNALRIL
TFLESTYIPP SYISEMEKAA KQGDTILVSG MKTGSSKLKA RIQEAVYKNV RPAEVRLLIL
ENILLNPAYD VYLLVGTSIH YKVQKIRQGK ITELSMPSDQ YELQLQNSIP DPQGDPARPV
AILTQDTSRV TAMQMGQSNL VLGHRSIRMQ GASRLPNSTI YVVEAGYLGF TVYPGDRWVL
ETGHLYAITI EVFDRSSNKV YPSDNIRIEA VLPAEFFEVL SSSQNGSYHH IRAIQSGQTA
ISATLTSVVD QDGGVHVLQV PVWNQQEVDI HIPITLYPSI LTFPWQPKTG AYQYTIKAHG
GSGNFSWSSS SSMVATVTVK GVMTTSGDTG LSVIRAHDVQ NPLHFGEMKV YVIEPSSMEF
APCQVEARVG HTLELPLTIS GFMPGGGSEV VTLSDCSHFD LVVEVENQGV FQPLPGRLPP
GPEHCSGVKV KADAQGSTTL LVSYTHGHVH LDAKITLAAY LPLKAVDPSS VAVVTLGSSK
EMLFEGGPRP WVLEPSKFFR NVTSEDTGSI SLSLLGPPAS RNYQQHRVLM TCQALGEQVI
ALSVGNRPSL SNPFPAVEPT VVKSICAPPS RLTLMPVYAL PQLDLSCPLL QQNKQVVPVS
SHRNPLLDLG AYDQQGRRFD NFSSLSIQWE SSRPLLASIE LDQPMQLVSQ DDGNGQKKLH
GLQTVSVHEA SGTTAISATA TGYQQSHLSE ARVKQPHDPL VPVSASIELI LVEDVRVSPE
EMTIYNHPGV QVELYITEGS GYFFLNTSTQ DIIKVAYQDT RGVALVHPLL PGSSTVMVHD
LCLAFPAPAK AIIHVSDIQE LYVRVVDKVE IGKAVKAYVR VLDFYKKPFL AKYFTFMDLK
LQAASQIITL VTLDEALDNY TATFLVHGVA IGQTSLSASV TDKSGQRVSS TPQQIEVFPP
FRLIPRKVTL IIGAMMQITS EGGPQPQSNI LFSINNESVA AVSSSGLVRG LMVGNGSVLG
VVQAVDAETG KVIIVSQDLV EVEVLQLQAV RIRAPITRMR TGTQMPVFVT GITSNQSPFS
FGNAVPGLTF HWSVTKRDVL DLRGRHHEVS IRLPPQYNFA MNVYGRVKGR TGLRVVVKAL
DPTAGQLHGL GKELSDEIQI QVFEKLRLLN PEIEAEQILM SPNSFIKLQT NRDGAAILSY
RVLDGPEKAP IVHTDEKGFL VSGSGIGVST LEVIAQEPFG TNQTILVAVK VSPVSYLRIS
MSPVLHTQHK EALTALPLGM TVTFIVHFHD SSGDIFHAHN SVLNFATNRD DFVQIGKGAT
NNTCIIRTVS VGLTLLHVWD VEHLGLSDFV PLPVLQAITP ELSGAVVVGD ILCLASVLTS
LGGVSGTWSS SASHVLYVDP KTGVAIARDA GSVTVYYEIA GQLKTFKEIV VGTPQKIVAR
RLHSAQTSIQ EATASKVTVS VGDRSSNLLG ECSPAQREAI EALHPESLIS CQLQFKQDVF
DFPACDVFTV EPGFDAALGQ YLCSVTMRRL TDKQLKHLNM KKTSLAVTAS IPSSYTSVEK
VGAEVPFSPG LYANQAEILL SNHYTSSEVK VFGAVESLEN LEVKSGSPAV LAFVKEKSFG
LPSFITYTVG VLDPTAGSQG PLSTALTFSS PATNQAITIP VTVAFVLDRR GPGPYGASLL
SHFLDSYQVM FFTFFALLAG TAVTIIAYHT VCAPRELASP LALTPRASPQ HSPHYLASSP
AAFNTLPSGR KASPPSGLWS PAYASH
