PAN2_MOUSE
ID PAN2_MOUSE Reviewed; 1200 AA.
AC Q8BGF7; Q3TZK5; Q68FH6; Q6ZQ63;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit Pan2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE EC=3.1.13.4 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 52 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE Short=PAN deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
GN Name=Pan2 {ECO:0000255|HAMAP-Rule:MF_03182}; Synonyms=Kiaa0710, Usp52;
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 [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [2]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Embryonic head, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain, and Eye;
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 [5]
RP FUNCTION.
RX PubMed=16284618; DOI=10.1038/nsmb1016;
RA Yamashita A., Chang T.-C., Yamashita Y., Zhu W., Zhong Z., Chen C.-Y.A.,
RA Shyu A.-B.;
RT "Concerted action of poly(A) nucleases and decapping enzyme in mammalian
RT mRNA turnover.";
RL Nat. Struct. Mol. Biol. 12:1054-1063(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18625844; DOI=10.1083/jcb.200801196;
RA Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B.;
RT "Deadenylation is prerequisite for P-body formation and mRNA decay in
RT mammalian cells.";
RL J. Cell Biol. 182:89-101(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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 INTERACTION WITH ZFP36.
RX PubMed=21078877; DOI=10.1128/mcb.00717-10;
RA Clement S.L., Scheckel C., Stoecklin G., Lykke-Andersen J.;
RT "Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA
RT decay by preventing deadenylase recruitment.";
RL Mol. Cell. Biol. 31:256-266(2011).
CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC complex, one of two cytoplasmic mRNA deadenylases involved in general
CC and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A)
CC tails of RNA and the activity is stimulated by poly(A)-binding protein
CC (PABP). PAN deadenylation is followed by rapid degradation of the
CC shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are
CC then degraded by two alternative mechanisms, namely exosome-mediated
CC 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA
CC decaping and subsequent 5'-3' exonucleolytic degradation by XRN1
CC (PubMed:16284618). Also acts as an important regulator of the HIF1A-
CC mediated hypoxic response. Required for HIF1A mRNA stability
CC independent of poly(A) tail length regulation (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:16284618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC domain. {ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC PAN3. {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC regulatory subunit PAN3 to form the poly(A)-nuclease (PAN)
CC deadenylation complex (By similarity). Interacts with ZFP36
CC (PubMed:21078877). {ECO:0000255|HAMAP-Rule:MF_03182,
CC ECO:0000269|PubMed:21078877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03182, ECO:0000269|PubMed:18625844}. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03182}. Note=Shuttles between nucleus and
CC cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BGF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGF7-2; Sequence=VSP_023752;
CC Name=3;
CC IsoId=Q8BGF7-3; Sequence=VSP_023750, VSP_023752;
CC Name=4;
CC IsoId=Q8BGF7-4; Sequence=VSP_023751;
CC -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
CC hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain
CC is predicted to be catalytically inactive because it lacks the active
CC site catalytic triad characteristic of thiol proteases, with residues
CC at the equivalent structural positions that are incompatible with
CC catalysis, and it cannot bind ubiquitin. It functions as a structural
CC scaffold for intra- and intermolecular interactions in the complex.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40
CC repeats and the pseudo-UCH domain mediates interaction with PAN3.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98006.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK129196; BAC98006.2; ALT_INIT; Transcribed_RNA.
DR EMBL; AK047887; BAC33183.1; -; mRNA.
DR EMBL; AK089001; BAC40693.1; -; mRNA.
DR EMBL; AK157800; BAE34203.1; -; mRNA.
DR EMBL; BC075686; AAH75686.1; -; mRNA.
DR EMBL; BC079841; AAH79841.1; -; mRNA.
DR CCDS; CCDS24271.1; -. [Q8BGF7-1]
DR CCDS; CCDS88107.1; -. [Q8BGF7-2]
DR CCDS; CCDS88108.1; -. [Q8BGF7-3]
DR RefSeq; NP_001239255.1; NM_001252326.1. [Q8BGF7-2]
DR RefSeq; NP_001239256.1; NM_001252327.1. [Q8BGF7-3]
DR RefSeq; NP_598753.1; NM_133992.3. [Q8BGF7-1]
DR AlphaFoldDB; Q8BGF7; -.
DR SMR; Q8BGF7; -.
DR BioGRID; 222025; 5.
DR IntAct; Q8BGF7; 1.
DR STRING; 10090.ENSMUSP00000005825; -.
DR MEROPS; C19.978; -.
DR iPTMnet; Q8BGF7; -.
DR PhosphoSitePlus; Q8BGF7; -.
DR EPD; Q8BGF7; -.
DR jPOST; Q8BGF7; -.
DR MaxQB; Q8BGF7; -.
DR PaxDb; Q8BGF7; -.
DR PeptideAtlas; Q8BGF7; -.
DR PRIDE; Q8BGF7; -.
DR ProteomicsDB; 287942; -. [Q8BGF7-1]
DR ProteomicsDB; 287943; -. [Q8BGF7-2]
DR ProteomicsDB; 287944; -. [Q8BGF7-3]
DR ProteomicsDB; 287945; -. [Q8BGF7-4]
DR Antibodypedia; 28142; 138 antibodies from 24 providers.
DR DNASU; 103135; -.
DR Ensembl; ENSMUST00000005825; ENSMUSP00000005825; ENSMUSG00000005682. [Q8BGF7-1]
DR Ensembl; ENSMUST00000218315; ENSMUSP00000151216; ENSMUSG00000005682. [Q8BGF7-2]
DR Ensembl; ENSMUST00000219721; ENSMUSP00000151874; ENSMUSG00000005682. [Q8BGF7-3]
DR GeneID; 103135; -.
DR KEGG; mmu:103135; -.
DR UCSC; uc007hme.2; mouse. [Q8BGF7-1]
DR UCSC; uc007hmf.2; mouse. [Q8BGF7-2]
DR UCSC; uc007hmg.2; mouse. [Q8BGF7-3]
DR CTD; 9924; -.
DR MGI; MGI:1918984; Pan2.
DR VEuPathDB; HostDB:ENSMUSG00000005682; -.
DR eggNOG; KOG1275; Eukaryota.
DR GeneTree; ENSGT00390000013978; -.
DR HOGENOM; CLU_002369_0_0_1; -.
DR InParanoid; Q8BGF7; -.
DR OMA; TQELLWT; -.
DR OrthoDB; 128953at2759; -.
DR PhylomeDB; Q8BGF7; -.
DR TreeFam; TF105657; -.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR BioGRID-ORCS; 103135; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Pan2; mouse.
DR PRO; PR:Q8BGF7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BGF7; protein.
DR Bgee; ENSMUSG00000005682; Expressed in secondary oocyte and 242 other tissues.
DR Genevisible; Q8BGF7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0031251; C:PAN complex; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; ISO:MGI.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; ISO:MGI.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
DR InterPro; IPR028881; PAN2_UCH_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Exonuclease; Hydrolase; Metal-binding;
KW mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..1200
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT Pan2"
FT /id="PRO_0000280522"
FT REPEAT 153..193
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 195..231
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 244..280
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 328..367
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 485..923
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 974..1146
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 368..484
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 977
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 979
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 1086
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 1138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q504Q3"
FT VAR_SEQ 95..112
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023750"
FT VAR_SEQ 687..722
FT /note="DKTGKNYDFAQVLKRSICLEQNTQAWCDNCEKYQPT -> GS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023751"
FT VAR_SEQ 826..834
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023752"
FT CONFLICT 175
FT /note="Q -> L (in Ref. 3; BAE34203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1200 AA; 135253 MW; 9CE98D3BE9FCE182 CRC64;
MNFEGLDPGL AEFSPAMHST LDPVLDAHLN PSLLQNVELD PEGVALEALP VQESVHIMEG
VYSELHSVVA EVGVPVSVSH FDLHEEMLWV GSHGGHATSF FGPALERYSS FQVNGGDDIR
QIQSLENGIL FLTKNNLKYM ARGGLIIFDY LLDENEDMHS VLLTDNSTLL VGGLQNHVLE
IDLNTVQETQ KYAVETPGVT IMRQTNRFFF CGHTSGKVSL RDLRSFKVEH EFDAFSGSLS
DFDVHGNLLA ACGFSSRLTG LACDRFLKVY DLRMMRAITP LQVHVDPAFL RFIPTYTSRL
AIISQSGQCQ FCEPTGLANP ADIFHVNPVG PLLMTFDVSA SKQALAFGDS EGCVHLWTDS
PEPSFNPYSR ETEFALPCLV DSLPPLDWSQ DLLPLSLIPV PLTTDALLSD WPAANSAPAP
RRAPPVDAEI LRTMKKVGFI GYAPNPRTRL RNQIPYRLKE SDHEFDNFSQ VTESPTGREE
EPLHTVSKKY RKVTIKYSKL GLEDFDFKHY NKTLFAGLEP HIPNAYCNCM IQVLYFLEPV
RCLIQNHLCQ KEFCLACELG FLFHMLDLSR GDPCQGSNFL RAFRTIPEAS ALGLILADSD
EASGKGSLAR LIQRWNRFIL TQLHQDMQEL EVPQAYRGAG GSFCSSGDSI IGQLFSCEME
NCSLCRCGSE TVRASSTLLF TLSYPEDKTG KNYDFAQVLK RSICLEQNTQ AWCDNCEKYQ
PTIQTRNIRH LPDILVINCE VNSSKEADFW RLQAEVAFKI AVKKYGGEMK SKEFALADRK
ELRSPEGFLC SSIEELKNVW LPFSIRMKMT KNKGLDVCNW ADEHELSSLG APSQWGPARA
EEELGVYVYD LMATVVHILD SRTGGSLVAH IKVGETYHQR KEGVTHQQWY LFNDFLIEPI
DKYEAVQFDM NWKVPAILYY VKRNLNSRYN LNIKNPIEAS VLLAEASLAR KQRKTHTTFI
PLMLNEMPQV GDLVGLDAEF VTLNEEEAEL RSDGTKSTIK PSQMSVARIT CVRGQGPNEG
IPFIDDYIST QEQVVDYLTQ YSGIKPGDLD AKISSKHLTT LKSTYLKLRF LIDIGVKFVG
HGLQKDFRVI NLMVPKDQVL DTVYLFHMPR KRMISLRFLA WYFLDLKIQG ETHDSIEDAR
TALQLYRKYL ELSKNGTEPE SFHKVLKGLY EKGRKMDWKV PEPESQTSPK NAAVFSVLAL
