PIN1_MOUSE
ID PIN1_MOUSE Reviewed; 165 AA.
AC Q9QUR7; Q543B3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1;
DE EC=5.2.1.8 {ECO:0000269|PubMed:29686383};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE Short=PPIase Pin1;
GN Name=Pin1;
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 [GENOMIC DNA / MRNA].
RX PubMed=10600477; DOI=10.1006/bbrc.1999.1736;
RA Fujimori F., Takahashi K., Uchida C., Uchida T.;
RT "Mice lacking Pin1 develop normally, but are defective in entering cell
RT cycle from G0 arrest.";
RL Biochem. Biophys. Res. Commun. 265:658-663(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, Kidney, and Oviduct;
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].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 INTERACTION WITH STIL.
RX PubMed=16024801; DOI=10.1128/mcb.25.15.6660-6672.2005;
RA Campaner S., Kaldis P., Izraeli S., Kirsch I.R.;
RT "Sil phosphorylation in a Pin1 binding domain affects the duration of the
RT spindle checkpoint.";
RL Mol. Cell. Biol. 25:6660-6672(2005).
RN [5]
RP FUNCTION IN BCL6 STABILITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17828269; DOI=10.1038/ni1508;
RA Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.;
RT "Genotoxic stress regulates expression of the proto-oncogene Bcl6 in
RT germinal center B cells.";
RL Nat. Immunol. 8:1132-1139(2007).
RN [6]
RP INTERACTION WITH PRKX.
RX PubMed=19367327; DOI=10.1038/ki.2009.95;
RA Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N.,
RA Wilson P.D.;
RT "Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney
RT development.";
RL Kidney Int. 76:54-62(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH IRAK3, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-73, AND DISRUPTION PHENOTYPE.
RX PubMed=29686383; DOI=10.1038/s41467-018-03886-6;
RA Nechama M., Kwon J., Wei S., Kyi A.T., Welner R.S., Ben-Dov I.Z.,
RA Arredouani M.S., Asara J.M., Chen C.H., Tsai C.Y., Nelson K.F.,
RA Kobayashi K.S., Israel E., Zhou X.Z., Nicholson L.K., Lu K.P.;
RT "The IL-33-PIN1-IRAK-M axis is critical for type 2 immunity in IL-33-
RT induced allergic airway inflammation.";
RL Nat. Commun. 9:1603-1603(2018).
CC -!- FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to
CC and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro)
CC motifs (PubMed:29686383). By inducing conformational changes in a
CC subset of phosphorylated proteins, acts as a molecular switch in
CC multiple cellular processes. Displays a preference for an acidic
CC residue N-terminal to the isomerized proline bond. Regulates mitosis
CC presumably by interacting with NIMA and attenuating its mitosis-
CC promoting activity. Down-regulates kinase activity of BTK. Can
CC transactivate multiple oncogenes and induce centrosome amplification,
CC chromosome instability and cell transformation. Required for the
CC efficient dephosphorylation and recycling of RAF1 after mitogen
CC activation (By similarity). Binds and targets PML and BCL6 for
CC degradation in a phosphorylation-dependent manner (PubMed:17828269).
CC Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7,
CC disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination
CC and degradation: degradation of FBXW7 leads to subsequent stabilization
CC of JUN (By similarity). May facilitate the ubiquitination and
CC proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-
CC protein ligase complex, hence favors DNA double-strand repair through
CC error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-
CC mediated homologous recombination (HR) (By similarity). Upon IL33-
CC induced lung inflammation, catalyzes cis-trans isomerization of
CC phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear
CC translocation and expression of pro-inflammatory genes in dendritic
CC cells (PubMed:29686383). {ECO:0000250|UniProtKB:Q13526,
CC ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:29686383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:29686383};
CC -!- SUBUNIT: Interacts with STIL (PubMed:16024801). Interacts with KIF20B.
CC Interacts with NEK6. Interacts (via WW domain) with PRKX
CC (PubMed:19367327). Interacts with BTK. Interacts (via PpiC domain) with
CC DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via
CC WW domain) with ATCAY; upon NGF stimulation. Interacts with PML.
CC Interacts with BCL6. Interacts with FBXW7, disrupting FBXW7
CC dimerization and promoting FBXW7 autoubiquitination and degradation (By
CC similarity). Directly interacts with RBBP8/CtIP; this interaction
CC depends upon RBBP8 phosphorylation (By similarity). Interacts (via WW
CC domain) with IRAK3/IRAK-M (when phosphorylated at 'Ser-110') in
CC response to IL33-mediated (but not TLR4 ligand LPS) dendritic cell
CC stimulation (PubMed:29686383). {ECO:0000250|UniProtKB:Q13526,
CC ECO:0000269|PubMed:16024801, ECO:0000269|PubMed:19367327,
CC ECO:0000269|PubMed:29686383}.
CC -!- INTERACTION:
CC Q9QUR7; Q8BUV3: Gphn; NbExp=6; IntAct=EBI-2432975, EBI-771218;
CC Q9QUR7; Q80Z64: Nanog; NbExp=2; IntAct=EBI-2432975, EBI-2312517;
CC Q9QUR7; P02340: Tp53; NbExp=3; IntAct=EBI-2432975, EBI-474016;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29686383}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q13526}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13526}. Note=Colocalizes with NEK6 in the
CC nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73
CC by DAPK1 results in inhibition of its nuclear localization.
CC {ECO:0000250|UniProtKB:Q13526}.
CC -!- TISSUE SPECIFICITY: Expressed in dendritic cells (at protein level).
CC {ECO:0000269|PubMed:29686383}.
CC -!- DOMAIN: The WW domain is required for the interaction with STIL and
CC KIF20B.
CC -!- PTM: Phosphorylation at Ser-73 by DAPK1 results in inhibition of its
CC catalytic activity, nuclear localization, and its ability to induce
CC centrosome amplification, chromosome instability and cell
CC transformation (By similarity). Ser-73 is dephosphorylated upon IL33-
CC stimulation of dendritic cells (PubMed:29686383).
CC {ECO:0000250|UniProtKB:Q13526, ECO:0000269|PubMed:29686383}.
CC -!- DISRUPTION PHENOTYPE: Animals display more and larger germinal centers
CC (PubMed:17828269). In response to intranasal administration of IL33,
CC lung inflammation is reduced compared to wild-type and is associated
CC with low infiltration by inflammatory cells, especially granulocytes, a
CC severe reduction in Th2-type cytokine secretion, including Il4, Il5 and
CC Il13 in bronchial alveolar fluids, and reduced up-regulation of Il6,
CC Csf3, Cxcl2 and Ccl5 mRNAs (PubMed:29686383). In addition, the increase
CC in IRAK3/IRAK-M protein levels in infiltrated inflammatory cells is
CC impaired (PubMed:29686383). In an ovalbumin-induced model of allergic
CC asthma, causes reduced lung inflammation and, reduced Th2-type cytokine
CC levels and inflammatory cell infiltration in bronchial alveolar fluids
CC (PubMed:29686383). {ECO:0000269|PubMed:17828269,
CC ECO:0000269|PubMed:29686383}.
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DR EMBL; AB009691; BAA87037.1; -; mRNA.
DR EMBL; AB009692; BAA87038.1; -; Genomic_DNA.
DR EMBL; AK002665; BAB22270.1; -; mRNA.
DR EMBL; AK003369; BAB22743.1; -; mRNA.
DR EMBL; AK054045; BAC35631.1; -; mRNA.
DR EMBL; AK150652; BAE29739.1; -; mRNA.
DR EMBL; AK160228; BAE35702.1; -; mRNA.
DR EMBL; BC038254; AAH38254.1; -; mRNA.
DR CCDS; CCDS22882.1; -.
DR PIR; JC7136; JC7136.
DR RefSeq; NP_075860.1; NM_023371.3.
DR AlphaFoldDB; Q9QUR7; -.
DR BMRB; Q9QUR7; -.
DR SMR; Q9QUR7; -.
DR BioGRID; 204839; 26.
DR DIP; DIP-44280N; -.
DR ELM; Q9QUR7; -.
DR IntAct; Q9QUR7; 6.
DR MINT; Q9QUR7; -.
DR STRING; 10090.ENSMUSP00000034689; -.
DR iPTMnet; Q9QUR7; -.
DR PhosphoSitePlus; Q9QUR7; -.
DR CPTAC; non-CPTAC-3863; -.
DR EPD; Q9QUR7; -.
DR jPOST; Q9QUR7; -.
DR MaxQB; Q9QUR7; -.
DR PaxDb; Q9QUR7; -.
DR PRIDE; Q9QUR7; -.
DR ProteomicsDB; 289575; -.
DR ABCD; Q9QUR7; 22 sequenced antibodies.
DR DNASU; 23988; -.
DR Ensembl; ENSMUST00000034689; ENSMUSP00000034689; ENSMUSG00000032171.
DR GeneID; 23988; -.
DR KEGG; mmu:23988; -.
DR UCSC; uc009ojd.1; mouse.
DR CTD; 5300; -.
DR MGI; MGI:1346036; Pin1.
DR VEuPathDB; HostDB:ENSMUSG00000032171; -.
DR eggNOG; KOG3259; Eukaryota.
DR GeneTree; ENSGT00640000091578; -.
DR HOGENOM; CLU_090028_0_1_1; -.
DR InParanoid; Q9QUR7; -.
DR OMA; DEVQCLH; -.
DR OrthoDB; 1437969at2759; -.
DR PhylomeDB; Q9QUR7; -.
DR TreeFam; TF101101; -.
DR BRENDA; 5.2.1.8; 3474.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
DR BioGRID-ORCS; 23988; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q9QUR7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9QUR7; protein.
DR Bgee; ENSMUSG00000032171; Expressed in primary motor cortex and 247 other tissues.
DR Genevisible; Q9QUR7; MM.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0016859; F:cis-trans isomerase activity; ISO:MGI.
DR GO; GO:0003774; F:cytoskeletal motor activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:ARUK-UCL.
DR GO; GO:0050815; F:phosphoserine residue binding; ISO:MGI.
DR GO; GO:0050816; F:phosphothreonine residue binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IMP:ParkinsonsUK-UCL.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase.
FT CHAIN 1..165
FT /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT 1"
FT /id="PRO_0000193436"
FT DOMAIN 5..39
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 54..165
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 33..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13526"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29686383"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13526"
SQ SEQUENCE 165 AA; 18370 MW; 188E95F009176B1F CRC64;
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGG STVGGSSKNG QGEPAKVRCS
HLLVKHSQSR RPSSWRQEKI TRSKEEALEL INGYIQKIKS GEEDFESLAS QFSDCSSAKA
RGDLGPFSRG QMQKPFEDAS FALRTGEMSG PVFTDSGIHI ILRTE
