ID   ECM29_MOUSE             Reviewed;        1840 AA.
AC   Q6PDI5; A2ALW0; Q6ZQC9; Q8BSW7; Q8CAH0; Q8R3M6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 4.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Proteasome adapter and scaffold protein ECM29 {ECO:0000305};
DE   AltName: Full=Proteasome-associated protein ECM29 homolog;
GN   Name=Ecpas {ECO:0000312|MGI:MGI:2140220};
GN   Synonyms=Ecm29, Kiaa0368 {ECO:0000303|PubMed:14621295};
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 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1449-1840 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Pituitary;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 612-1840 (ISOFORMS 1/2).
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15496406; DOI=10.1074/jbc.m410444200;
RA   Gorbea C., Goellner G.M., Teter K., Holmes R.K., Rechsteiner M.;
RT   "Characterization of mammalian Ecm29, a 26 S proteasome-associated protein
RT   that localizes to the nucleus and membrane vesicles.";
RL   J. Biol. Chem. 279:54849-54861(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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).
RN   [7]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=26802743; DOI=10.1093/jb/mvw006;
RA   Haratake K., Sato A., Tsuruta F., Chiba T.;
RT   "KIAA0368-deficiency affects disassembly of 26S proteasome under oxidative
RT   stress condition.";
RL   J. Biochem. 159:609-618(2016).
CC   -!- FUNCTION: Adapter/scaffolding protein that binds to the 26S proteasome,
CC       motor proteins and other compartment specific proteins. May couple the
CC       proteasome to different compartments including endosome, endoplasmic
CC       reticulum and centrosome. May play a role in ERAD and other enhanced
CC       proteolysis (By similarity). Promotes proteasome dissociation under
CC       oxidative stress (PubMed:26802743). {ECO:0000250|UniProtKB:Q5VYK3,
CC       ECO:0000269|PubMed:26802743}.
CC   -!- SUBUNIT: Non-stoichiometric component of the proteasome; associates
CC       with the 26S proteasome. Interacts (via N-terminus) with VPS11, VPS26A,
CC       VPS36, RAB11FIP4 and RABEP1. Interacts (via C-terminus) with DCTN1,
CC       DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6.
CC       {ECO:0000250|UniProtKB:Q5VYK3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q5VYK3}. Endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000250|UniProtKB:Q5VYK3}. Endosome
CC       {ECO:0000250|UniProtKB:Q5VYK3}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q5VYK3}. Nucleus
CC       {ECO:0000250|UniProtKB:Q5VYK3}. Endosome, multivesicular body
CC       {ECO:0000250|UniProtKB:Q5VYK3}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q5VYK3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=Q6PDI5-2; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q6PDI5-1; Sequence=VSP_062174;
CC       Name=3;
CC         IsoId=Q6PDI5-3; Sequence=VSP_062175, VSP_062176;
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC       {ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:26802743}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice are viable, fertile, and do not
CC       show any histological abnormalities. Under stressed condition, 26S
CC       proteasome dissociates in wild-type cells, but not in cells from
CC       deficient mice. {ECO:0000269|PubMed:26802743}.
CC   -!- SIMILARITY: Belongs to the ECM29 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25035.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK030369; BAC26926.1; -; mRNA.
DR   EMBL; AK038775; BAC30129.1; -; mRNA.
DR   EMBL; AL805972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL806535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025035; AAH25035.1; ALT_INIT; mRNA.
DR   EMBL; BC058684; AAH58684.1; -; mRNA.
DR   EMBL; AK129127; BAC97937.1; -; mRNA.
DR   CCDS; CCDS18214.1; -. [Q6PDI5-2]
DR   RefSeq; NP_759013.2; NM_172381.2. [Q6PDI5-1]
DR   RefSeq; XP_006537911.1; XM_006537848.3. [Q6PDI5-2]
DR   RefSeq; XP_006537912.1; XM_006537849.3.
DR   AlphaFoldDB; Q6PDI5; -.
DR   BioGRID; 230950; 44.
DR   IntAct; Q6PDI5; 6.
DR   STRING; 10090.ENSMUSP00000099953; -.
DR   GlyConnect; 2618; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q6PDI5; 1 site, 2 glycans.
DR   GlyGen; Q6PDI5; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; Q6PDI5; -.
DR   PhosphoSitePlus; Q6PDI5; -.
DR   SwissPalm; Q6PDI5; -.
DR   CPTAC; non-CPTAC-3973; -.
DR   EPD; Q6PDI5; -.
DR   jPOST; Q6PDI5; -.
DR   MaxQB; Q6PDI5; -.
DR   PaxDb; 10090-ENSMUSP00000099953; -.
DR   PeptideAtlas; Q6PDI5; -.
DR   ProteomicsDB; 277437; -. [Q6PDI5-1]
DR   ProteomicsDB; 277438; -. [Q6PDI5-2]
DR   Pumba; Q6PDI5; -.
DR   Antibodypedia; 29523; 56 antibodies from 15 providers.
DR   DNASU; 230249; -.
DR   Ensembl; ENSMUST00000102889.10; ENSMUSP00000099953.4; ENSMUSG00000050812.19. [Q6PDI5-1]
DR   Ensembl; ENSMUST00000107557.9; ENSMUSP00000103182.3; ENSMUSG00000050812.19. [Q6PDI5-3]
DR   GeneID; 230249; -.
DR   KEGG; mmu:230249; -.
DR   UCSC; uc008sze.1; mouse. [Q6PDI5-2]
DR   UCSC; uc008szf.1; mouse. [Q6PDI5-2]
DR   AGR; MGI:2140220; -.
DR   CTD; 23392; -.
DR   MGI; MGI:2140220; Ecpas.
DR   VEuPathDB; HostDB:ENSMUSG00000050812; -.
DR   eggNOG; KOG0915; Eukaryota.
DR   GeneTree; ENSGT00940000153612; -.
DR   HOGENOM; CLU_000880_2_0_1; -.
DR   InParanoid; Q6PDI5; -.
DR   OMA; CRIKDIE; -.
DR   OrthoDB; 1060702at2759; -.
DR   PhylomeDB; Q6PDI5; -.
DR   TreeFam; TF314213; -.
DR   BioGRID-ORCS; 230249; 4 hits in 77 CRISPR screens.
DR   PRO; PR:Q6PDI5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q6PDI5; Protein.
DR   Bgee; ENSMUSG00000050812; Expressed in hindlimb stylopod muscle and 259 other cell types or tissues.
DR   ExpressionAtlas; Q6PDI5; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005770; C:late endosome; ISO:MGI.
DR   GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; ISO:MGI.
DR   GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024372; Ecm29.
DR   PANTHER; PTHR23346:SF19; PROTEASOME ADAPTER AND SCAFFOLD PROTEIN ECM29; 1.
DR   PANTHER; PTHR23346; TRANSLATIONAL ACTIVATOR GCN1-RELATED; 1.
DR   Pfam; PF13001; Ecm29; 1.
DR   SUPFAM; SSF48371; ARM repeat; 3.
DR   Genevisible; Q6PDI5; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Endoplasmic reticulum; Endosome; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..1840
FT                   /note="Proteasome adapter and scaffold protein ECM29"
FT                   /id="PRO_0000212560"
FT   REPEAT          28..65
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   REPEAT          107..144
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   REPEAT          162..206
FT                   /note="HEAT 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   REPEAT          327..363
FT                   /note="HEAT 4"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   REPEAT          388..427
FT                   /note="HEAT 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          430..467
FT                   /note="HEAT 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          470..508
FT                   /note="HEAT 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          684..721
FT                   /note="HEAT 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          722..760
FT                   /note="HEAT 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          784..821
FT                   /note="HEAT 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          830..869
FT                   /note="HEAT 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          871..908
FT                   /note="HEAT 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          932..970
FT                   /note="HEAT 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          976..1013
FT                   /note="HEAT 14"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1014..1051
FT                   /note="HEAT 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1113..1150
FT                   /note="HEAT 16"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1153..1190
FT                   /note="HEAT 17"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1195..1232
FT                   /note="HEAT 18"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1244..1282
FT                   /note="HEAT 19"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1286..1324
FT                   /note="HEAT 20"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1349..1387
FT                   /note="HEAT 21"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1391..1428
FT                   /note="HEAT 22"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1518..1555
FT                   /note="HEAT 23"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1559..1596
FT                   /note="HEAT 24"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1606..1643
FT                   /note="HEAT 25"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1647..1684
FT                   /note="HEAT 26"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1780..1823
FT                   /note="HEAT 27"
FT                   /evidence="ECO:0000255"
FT   REGION          187..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   MOD_RES         831
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   CROSSLNK        1034
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT   VAR_SEQ         1..7
FT                   /note="MYHIDCR -> METGSDS (in isoform 1)"
FT                   /id="VSP_062174"
FT   VAR_SEQ         886..942
FT                   /note="AKQIELQFTIGEAITSAAIGTNSVAARDAWLVTEEEYIPPAGAKVNDVVPWV
FT                   LDVIL -> VLIFLIIQIKCIFSCFAYYQILDVCYWEVINLLSVSVLSPACSANRYQKW
FT                   ALDPLKL (in isoform 3)"
FT                   /id="VSP_062175"
FT   VAR_SEQ         943..1840
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_062176"
FT   CONFLICT        1446
FT                   /note="D -> E (in Ref. 3; AAH25035 and 4; BAC97937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1449
FT                   /note="V -> F (in Ref. 4; BAC26926)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1840 AA;  203915 MW;  447D913AA8B0C19E CRC64;
     MYHIDCRDQL ERVFLRLGHA ETDEQLQNII SKFLPPVLLK LSSTQEGVRK KVMELLVHLN
     KRIKSRPKIQ LPVETLLVQY QDPAAVSFVT NFTIIYVKMG YPRLPVEKQC ELAPTLLTAM
     EGKPQPQQDS LMHLLIPTLF HMKYPAESSK SASPFNLAEK PKTVQLLLDF MLDVLLMPYG
     YVLNESQSRQ NSSSSSQGSS SNSGGGSGIP QPPPGMSFYA AKRVIGDNPW TPEQLEQCKL
     GIVKFIEAEQ VPELEAVLHL VIASSDTRHS VATAADLELK SKQSLIDWNN PAIINKMYKV
     YLGDIPLKTK EGAVLKPELK RDPVSTRVKL KIVPHLLRSR QAAETFPANI QVVYDGLFGT
     NTNSKLRTLS LQFVHHICLT CPEIKIKPLG PMLLNGLTKL INEYKEDPKL LSMAYSAVGK
     LSSRMPHLFT KDIALVQQLF EALCKEEPET RLAIQEALSM MVGAYSTLEG AQRTLMEALV
     ASYLIKPEVQ VRQVAVKFAS TVFPSDHIPS RYLLLLAAGD PREEVHGEAQ RVLRCLPGRN
     KKESASKQMP SFPEMVYYIQ EKASHRMKTP VKYMTGTTVL PFNPAAFGEI VLYLRMCLAH
     SAGVVPTSQS LADMQDHAPA IGRYIRALMS SSQATASSSN KSGETNPVQI YTGLLQQLLA
     GVGGLPVMYC LLEAVSVYPE KLATKFVDKT EWIKSLMSSS KEEMRELAAL FYSVVVSTVS
     GIELKSMIEQ LIKATKDNHS PEVQHGSLLA LGFTVGRYLA KKRVRMAEQH DLETDADLLP
     EQEEIIRSAT ETIGSFLDST SPLLAIAACT ALGEIGRNGP LPIPSEGSGF TKLHLVESLL
     NRIPSSKETN KMKERAIQTL GYFPVGDGVF PHQKLLLQGL MDSVEAKQIE LQFTIGEAIT
     SAAIGTNSVA ARDAWLVTEE EYIPPAGAKV NDVVPWVLDV ILNKHIISPN PHVRQAACIW
     LLSLVRKLST HREVKSHLKE IQSAFVSVLS ENDELSQDVA SKGLGLVYEL GNEQDQQELV
     STLVETLMTG KRVKHEVSGE TVVFQGGGLG KTPDGQGLST YKELCSLASD LSQPDLVYKF
     MNLANHHAMW NSRKGAAFGF NVIATRAGEQ LAPFLPQLVP RLYRYQFDPN LGIRQAMTSI
     WNALVTDKSM VDKYLKEILQ DLIKNLTSNM WRVRESSCLA LNDLLRGRPL DDVIDKLPEM
     WETLFRVQDD IKESVRKAAE LALKTLSKVC VKMCDPAKGA AGQRTIAVLL PCLLDKGMMS
     PVTEVRALSI NTLVKISKSA GAMLKPHAPK LIPALLESLS VLEPQVLNYL SLRATEQEKD
     VMDSARLSAA KSSPMMETIN MCLQYLDVSV LGELVPRLCE LIRSGVGLGT KGGCASVIVS
     LTTQCPQDLT PYSGKLMSAL LSGLTDRNSV IQKSCAFAMG HLVRTSRDSS TEKLLQKLNG
     WYMEKDEPVY KTSCALTIHA IGRYSPDVLK NHAKEVLPLA FLGMHEIADE EKSEKEECNM
     WTEVWQENVP GSFGGIRLYL QELITITQKA LQSQSWKMKA QGAIAMASIS KQTSSLVPPY
     LGMILSALMQ GLAGRTWAGK EELLKAIACV VTACSTELEK SVPNQPTTNE ILQAVLKECC
     KENLKYKIVA ISCAADVLKA TKEDRFQEFS DIVIPLIKKN SLESMGVRTT KAEDENEKER
     ELQLESLLGA FESLGKAWPR NPDTQRCYRQ ELCKLMCERL RLSTWKVQLG VLQSMNAFFQ
     GLMLLEEEHA DPEALAEILL ETCKSITYSL ENKTYSSVRT EALSVVELLL KKLEEAKQWE
     SLTAECRGLL IESLATMETD NRPELQEKAS VLKKTLESLE
//