TPC12_HUMAN
ID TPC12_HUMAN Reviewed; 735 AA.
AC Q8WVT3; B3KV01; D6W4Y2; Q8WVW1; Q9Y395;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Trafficking protein particle complex subunit 12 {ECO:0000305};
DE AltName: Full=Tetratricopeptide repeat protein 15 {ECO:0000303|PubMed:21525244};
DE Short=TPR repeat protein 15 {ECO:0000303|PubMed:21525244};
DE Short=TTC-15 {ECO:0000303|PubMed:21525244};
DE AltName: Full=Trafficking of membranes and mitosis {ECO:0000303|PubMed:25918224};
GN Name=TRAPPC12 {ECO:0000312|HGNC:HGNC:24284};
GN Synonyms=TRAMM {ECO:0000303|PubMed:25918224},
GN TTC15 {ECO:0000303|PubMed:21525244};
GN ORFNames=CGI-87 {ECO:0000303|PubMed:10810093};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-301.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
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 356-735.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, IDENTIFICATION IN TRAPP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21525244; DOI=10.1091/mbc.e10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early
RT stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPE, AND
RP PHOSPHORYLATION.
RX PubMed=25918224; DOI=10.1083/jcb.201501090;
RA Milev M.P., Hasaj B., Saint-Dic D., Snounou S., Zhao Q., Sacher M.;
RT "TRAMM/TrappC12 plays a role in chromosome congression, kinetochore
RT stability, and CENP-E recruitment.";
RL J. Cell Biol. 209:221-234(2015).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-717.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP INVOLVEMENT IN PEBAS, AND VARIANT PEBAS VAL-627.
RX PubMed=28777934; DOI=10.1016/j.ajhg.2017.07.006;
RA Milev M.P., Grout M.E., Saint-Dic D., Cheng Y.H., Glass I.A., Hale C.J.,
RA Hanna D.S., Dorschner M.O., Prematilake K., Shaag A., Elpeleg O.,
RA Sacher M., Doherty D., Edvardson S.;
RT "Mutations in TRAPPC12 manifest in progressive childhood encephalopathy and
RT Golgi dysfunction.";
RL Am. J. Hum. Genet. 101:291-299(2017).
CC -!- FUNCTION: Component of the TRAPP complex, which is involved in
CC endoplasmic reticulum to Golgi apparatus trafficking at a very early
CC stage (PubMed:21525244, PubMed:28777934). Also plays a role in
CC chromosome congression, kinetochore assembly and stability and controls
CC the recruitment of CENPE to the kinetochores (PubMed:25918224).
CC {ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:25918224,
CC ECO:0000269|PubMed:28777934}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC TRAPPC12 (PubMed:21525244). Interacts with CENPE (PubMed:25918224).
CC {ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:25918224}.
CC -!- INTERACTION:
CC Q8WVT3; O00327-8: ARNTL; NbExp=3; IntAct=EBI-2819919, EBI-11991546;
CC Q8WVT3; I6L957: HNRNPA2B1; NbExp=3; IntAct=EBI-2819919, EBI-1642515;
CC Q8WVT3; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-2819919, EBI-821335;
CC Q8WVT3; Q96LW2: RSKR; NbExp=3; IntAct=EBI-2819919, EBI-1054572;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:21525244}. Nucleus
CC {ECO:0000269|PubMed:25918224}. Note=Mainly localizes to structures
CC resembling the Golgi and a small amount is found in the nucleus.
CC {ECO:0000269|PubMed:25918224}.
CC -!- PTM: Phosphorylated as the cells enter mitosis but is dephosphorylated
CC at or before the onset of anaphase. The phosphorylated form recruits
CC CENPE to kinetochores more efficiently than the non-phosphorylated
CC form. {ECO:0000269|PubMed:25918224}.
CC -!- DISEASE: Encephalopathy, progressive, early-onset, with brain atrophy
CC and spasticity (PEBAS) [MIM:617669]: An autosomal recessive,
CC progressive encephalopathy characterized by central nervous system
CC atrophy and dysfunction, spasticity, microcephaly, global developmental
CC delay, and hearing loss. {ECO:0000269|PubMed:28777934}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Cells display a fragmented Golgi apparatus (PubMed:28777934).
CC {ECO:0000269|PubMed:28777934}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34082.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK098327; BAG53613.1; -; mRNA.
DR EMBL; CH471053; EAX01067.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01068.1; -; Genomic_DNA.
DR EMBL; BC014164; AAH14164.2; -; mRNA.
DR EMBL; BC017475; AAH17475.2; -; mRNA.
DR EMBL; AF151845; AAD34082.1; ALT_INIT; mRNA.
DR CCDS; CCDS1652.1; -.
DR RefSeq; NP_001308031.1; NM_001321102.1.
DR RefSeq; NP_057114.5; NM_016030.5.
DR AlphaFoldDB; Q8WVT3; -.
DR SMR; Q8WVT3; -.
DR BioGRID; 119301; 95.
DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR CORUM; Q8WVT3; -.
DR DIP; DIP-48283N; -.
DR IntAct; Q8WVT3; 26.
DR STRING; 9606.ENSP00000324318; -.
DR iPTMnet; Q8WVT3; -.
DR MetOSite; Q8WVT3; -.
DR PhosphoSitePlus; Q8WVT3; -.
DR BioMuta; TRAPPC12; -.
DR DMDM; 116242834; -.
DR EPD; Q8WVT3; -.
DR jPOST; Q8WVT3; -.
DR MassIVE; Q8WVT3; -.
DR MaxQB; Q8WVT3; -.
DR PaxDb; Q8WVT3; -.
DR PeptideAtlas; Q8WVT3; -.
DR PRIDE; Q8WVT3; -.
DR ProteomicsDB; 74819; -.
DR Antibodypedia; 26298; 68 antibodies from 15 providers.
DR DNASU; 51112; -.
DR Ensembl; ENST00000324266.10; ENSP00000324318.5; ENSG00000171853.16.
DR Ensembl; ENST00000382110.6; ENSP00000371544.2; ENSG00000171853.16.
DR GeneID; 51112; -.
DR KEGG; hsa:51112; -.
DR MANE-Select; ENST00000324266.10; ENSP00000324318.5; NM_016030.6; NP_057114.5.
DR UCSC; uc002qxm.2; human.
DR CTD; 51112; -.
DR DisGeNET; 51112; -.
DR GeneCards; TRAPPC12; -.
DR HGNC; HGNC:24284; TRAPPC12.
DR HPA; ENSG00000171853; Tissue enhanced (testis).
DR MalaCards; TRAPPC12; -.
DR MIM; 614139; gene.
DR MIM; 617669; phenotype.
DR neXtProt; NX_Q8WVT3; -.
DR OpenTargets; ENSG00000171853; -.
DR Orphanet; 500144; Early-onset progressive encephalopathy-hearing loss-pons hypoplasia-brain atrophy syndrome.
DR PharmGKB; PA134944710; -.
DR VEuPathDB; HostDB:ENSG00000171853; -.
DR eggNOG; KOG2796; Eukaryota.
DR GeneTree; ENSGT00390000002448; -.
DR HOGENOM; CLU_014917_0_0_1; -.
DR InParanoid; Q8WVT3; -.
DR OMA; FNAQCLK; -.
DR OrthoDB; 1142416at2759; -.
DR PhylomeDB; Q8WVT3; -.
DR TreeFam; TF320881; -.
DR PathwayCommons; Q8WVT3; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q8WVT3; -.
DR BioGRID-ORCS; 51112; 32 hits in 1075 CRISPR screens.
DR ChiTaRS; TRAPPC12; human.
DR GenomeRNAi; 51112; -.
DR Pharos; Q8WVT3; Tbio.
DR PRO; PR:Q8WVT3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WVT3; protein.
DR Bgee; ENSG00000171853; Expressed in left testis and 93 other tissues.
DR ExpressionAtlas; Q8WVT3; baseline and differential.
DR Genevisible; Q8WVT3; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; IMP:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0090234; P:regulation of kinetochore assembly; IMP:UniProtKB.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Deafness; Disease variant; ER-Golgi transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..735
FT /note="Trafficking protein particle complex subunit 12"
FT /id="PRO_0000106401"
FT REPEAT 545..578
FT /note="TPR 1"
FT REPEAT 580..613
FT /note="TPR 2"
FT REPEAT 620..653
FT /note="TPR 3"
FT REPEAT 654..687
FT /note="TPR 4"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2L8"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 301
FT /note="S -> G (in dbSNP:rs11686212)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_028442"
FT VARIANT 627
FT /note="A -> V (in PEBAS; unknown pathological significance;
FT dbSNP:rs768950892)"
FT /evidence="ECO:0000269|PubMed:28777934"
FT /id="VAR_080390"
FT VARIANT 717
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035869"
FT CONFLICT 451
FT /note="F -> V (in Ref. 4; AAD34082)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="E -> D (in Ref. 4; AAD34082)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="E -> D (in Ref. 3; AAH14164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 79375 MW; B844FB3749866E3F CRC64;
MEDAGGGEET PAPEAPHPPQ LAPPEEQGLL FQEETIDLGG DEFGSEENET ASEGSSPLAD
KLNEHMMESV LISDSPNSEG DAGDLGRVRD EAEPGGEGDP GPEPAGTPSP SGEADGDCAP
EDAAPSSGGA PRQDAAREVP GSEAARPEQE PPVAEPVPVC TIFSQRAPPA SGDGFEPQMV
KSPSFGGASE ASARTPPQVV QPSPSLSTFF GDTAASHSLA SDFFDSFTTS AFISVSNPGA
GSPAPASPPP LAVPGTEGRP EPVAMRGPQA AAPPASPEPF AHIQAVFAGS DDPFATALSM
SEMDRRNDAW LPGEATRGVL RAVATQQRGA VFVDKENLTM PGLRFDNIQG DAVKDLMLRF
LGEKAAAKRQ VLNADSVEQS FVGLKQLISC RNWRAAVDLC GRLLTAHGQG YGKSGLLTSH
TTDSLQLWFV RLALLVKLGL FQNAEMEFEP FGNLDQPDLY YEYYPHVYPG RRGSMVPFSM
RILHAELQQY LGNPQESLDR LHKVKTVCSK ILANLEQGLA EDGGMSSVTQ EGRQASIRLW
RSRLGRVMYS MANCLLLMKD YVLAVEAYHS VIKYYPEQEP QLLSGIGRIS LQIGDIKTAE
KYFQDVEKVT QKLDGLQGKI MVLMNSAFLH LGQNNFAEAH RFFTEILRMD PRNAVANNNA
AVCLLYLGKL KDSLRQLEAM VQQDPRHYLH ESVLFNLTTM YELESSRSMQ KKQALLEAVA
GKEGDSFNTQ CLKLA
