ID   TERA_PIG                Reviewed;         806 AA.
AC   P03974;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Transitional endoplasmic reticulum ATPase;
DE            Short=TER ATPase;
DE            EC=3.6.4.6 {ECO:0000250|UniProtKB:P55072};
DE   AltName: Full=15S Mg(2+)-ATPase p97 subunit;
DE   AltName: Full=Valosin-containing protein;
DE            Short=VCP;
GN   Name=VCP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3468358; DOI=10.1038/325542a0;
RA   Koller K.J., Brownstein M.J.;
RT   "Use of a cDNA clone to identify a supposed precursor protein containing
RT   valosin.";
RL   Nature 325:542-545(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 493-517.
RX   PubMed=4054310; DOI=10.1016/0014-5793(85)80021-1;
RA   Schmidt W.E., Mutt V., Carlquist M., Kratzin H., Conlon J.M.,
RA   Creutzfeldt W.;
RT   "Valosin: isolation and characterization of a novel peptide from porcine
RT   intestine.";
RL   FEBS Lett. 191:264-268(1985).
RN   [3]
RP   SHOWS THAT VALOSIN IS A PURIFICATION ARTIFACT.
RX   PubMed=2927256; DOI=10.1016/0024-3205(89)90464-5;
RA   Gill J.S., Ghatei M.A., Domin J., Bloom S.R.;
RT   "The generation of valosin-like peptides from a precursor protein in vitro
RT   as an extraction artifact.";
RL   Life Sci. 44:483-491(1989).
CC   -!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
CC       mitosis and for their reassembly after mitosis. Involved in the
CC       formation of the transitional endoplasmic reticulum (tER). The transfer
CC       of membranes from the endoplasmic reticulum to the Golgi apparatus
CC       occurs via 50-70 nm transition vesicles which derive from part-rough,
CC       part-smooth transitional elements of the endoplasmic reticulum (tER).
CC       Vesicle budding from the tER is an ATP-dependent process. The ternary
CC       complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins
CC       and is necessary for the export of misfolded proteins from the ER to
CC       the cytoplasm, where they are degraded by the proteasome. The NPLOC4-
CC       UFD1-VCP complex regulates spindle disassembly at the end of mitosis
CC       and is necessary for the formation of a closed nuclear envelope.
CC       Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of
CC       the VCP/p97-AMFR/gp78 complex that participates in the final step of
CC       the sterol-mediated ubiquitination and endoplasmic reticulum-associated
CC       degradation (ERAD) of HMGCR. Mediates the endoplasmic reticulum-
CC       associated degradation of CHRNA3 in cortical neurons as part of the
CC       STUB1-VCP-UBXN2A complex (By similarity). Involved in endoplasmic
CC       reticulum stress-induced pre-emptive quality control, a mechanism that
CC       selectively attenuates the translocation of newly synthesized proteins
CC       into the endoplasmic reticulum and reroutes them to the cytosol for
CC       proteasomal degradation. Involved in clearance process by mediating
CC       G3BP1 extraction from stress granules. Also involved in DNA damage
CC       response: recruited to double-strand breaks (DSBs) sites in a RNF8- and
CC       RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA
CC       damage sites. Recruited to stalled replication forks by SPRTN: may act
CC       by mediating extraction of DNA polymerase eta (POLH) to prevent
CC       excessive translesion DNA synthesis and limit the incidence of
CC       mutations induced by DNA damage. Together with SPRTN metalloprotease,
CC       involved in the repair of covalent DNA-protein cross-links (DPCs)
CC       during DNA synthesis. Involved in interstrand cross-link repair in
CC       response to replication stress by mediating unloading of the
CC       ubiquitinated CMG helicase complex. Mediates extraction of PARP1
CC       trapped to chromatin: recognizes and binds ubiquitinated PARP1 and
CC       promotes its removal. Required for cytoplasmic retrotranslocation of
CC       stressed/damaged mitochondrial outer-membrane proteins and their
CC       subsequent proteasomal degradation. Essential for the maturation of
CC       ubiquitin-containing autophagosomes and the clearance of ubiquitinated
CC       protein by autophagy. Acts as a negative regulator of type I interferon
CC       production by interacting with RIGI: interaction takes place when RIGI
CC       is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains,
CC       leading to recruit RNF125 and promote ubiquitination and degradation of
CC       RIGI. May play a role in the ubiquitin-dependent sorting of membrane
CC       proteins to lysosomes where they undergo degradation. May more
CC       particularly play a role in caveolins sorting in cells. By controlling
CC       the steady-state expression of the IGF1R receptor, indirectly regulates
CC       the insulin-like growth factor receptor signaling pathway (By
CC       similarity). {ECO:0000250|UniProtKB:P23787,
CC       ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC         Evidence={ECO:0000250|UniProtKB:P55072};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter,
CC       that displays 6-fold radial symmetry. Part of a ternary complex
CC       containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds
CC       to one end of a VCP homohexamer. The complex binds to membranes
CC       enriched in phosphatidylethanolamine-containing lipids and promotes
CC       Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1,
CC       binding to this heterodimer inhibits Golgi-membrane fusion. Interaction
CC       with VCIP135 leads to dissociation of the complex via ATP hydrolysis by
CC       VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP.
CC       Interacts with NSFL1C-like protein p37; the complex has membrane fusion
CC       activity and is required for Golgi and endoplasmic reticulum
CC       biogenesis. Interacts with SELENOS and SYVN1, as well as with DERL1
CC       (via SHP-box motif), DERL2 and DERL3; which probably transfer misfolded
CC       proteins from the ER to VCP. Interacts with SVIP. Component of a
CC       complex required to couple retrotranslocation, ubiquitination and
CC       deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Part of
CC       a complex composed of STUB1/CHIP, VCP/p97, CHRNA3, and UBXN2A that
CC       modulates the ubiquitination and endoplasmic reticulum-associated
CC       degradation (ERAD) of CHRNA3 (By similarity). Within the complex UBXN2A
CC       acts as a scaffold protein required for the interaction of CHRNA3 with
CC       VCP/p97, this interaction also inhibits CHRNA3 ubiquitination by
CC       STUB1/CHIP and subsequently ERAD (By similarity). Interacts with UBXN2A
CC       (via UBX domain); the interaction is required for the interaction of
CC       CHRNA3 in the STUB1-VCP-UBXN2A complex (By similarity). Directly
CC       interacts with UBXN4 and RNF19A. Interacts with CASR. Interacts with
CC       UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103.
CC       Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78
CC       complex that participates in the final step of the endoplasmic
CC       reticulum-associated degradation (ERAD) of HMGCR. Interacts directly
CC       with AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-terminal
CC       domain). Interacts with SPRTN; leading to recruitment to stalled
CC       replication forks. Interacts with WASHC5. Interacts with UBOX5.
CC       Interacts (via N-terminus) with UBXN7, UBXN8, and probably several
CC       other UBX domain-containing proteins (via UBX domains); the
CC       interactions are mutually exclusive with VIM-dependent interactions
CC       such as those with AMFR and SELENOS. Forms a complex with UBQLN1 and
CC       UBXN4. Interacts (via the PIM motif) with RNF31 (via the PUB domain).
CC       Interacts with RIGI and RNF125; interaction takes place when RIGI is
CC       ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains,
CC       leading to recruit RNF125 and promote ubiquitination and degradation of
CC       RIGI. Interacts with BAG6. Interacts with UBXN10. Interacts with UBXN6;
CC       the interaction with UBXN6 is direct and competitive with UFD1. Forms a
CC       ternary complex with CAV1 and UBXN6. Interacts with PLAA, UBXN6 and
CC       YOD1; may form a complex involved in macroautophagy. Interacts with
CC       ANKZF1. Interacts with ubiquitin-binding protein FAF1. Interacts with
CC       ZFAND2B (via VIM motif); the interaction is direct. Interacts with
CC       ZFAND1 (via its ubiquitin-like region); this interaction occurs in an
CC       arsenite-dependent manner (By similarity). Interacts with CCDC47 (By
CC       similarity). Interacts with LMBR1L and UBAC2 (By similarity). Interacts
CC       with ATXN3 (By similarity). Interacts with TEX264; bridging VCP to
CC       covalent DNA-protein cross-links (DPCs) (By similarity).
CC       {ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072,
CC       ECO:0000250|UniProtKB:Q01853}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}.
CC       Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}.
CC       Note=Recruited to the cytoplasmic surface of the endoplasmic reticulum
CC       via interaction with AMFR/gp78. Following DNA double-strand breaks,
CC       recruited to the sites of damage. Recruited to stalled replication
CC       forks via interaction with SPRTN. Recruited to damaged lysosomes
CC       decorated with K48-linked ubiquitin chains. Colocalizes with TIA1,
CC       ZFAND1 and G3BP1 in cytoplasmic stress granules (SGs) in response to
CC       arsenite-induced stress treatment (By similarity).
CC       {ECO:0000250|UniProtKB:P55072}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P55072}.
CC   -!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the
CC       presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity.
CC       {ECO:0000250|UniProtKB:P55072}.
CC   -!- PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen
CC       receptor activation. Phosphorylated in mitotic cells.
CC       {ECO:0000250|UniProtKB:P46462}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- CAUTION: Valosin is an artifact of purification procedure, generated in
CC       vitro by cleavage of the whole protein upon acid extraction of tissues.
CC       {ECO:0000305}.
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DR   EMBL; M30143; AAA31142.1; -; mRNA.
DR   PIR; A26360; VPPG.
DR   RefSeq; NP_999445.1; NM_214280.1.
DR   AlphaFoldDB; P03974; -.
DR   SMR; P03974; -.
DR   BioGRID; 1149651; 1.
DR   STRING; 9823.ENSSSCP00000035359; -.
DR   PaxDb; 9823-ENSSSCP00000005692; -.
DR   PeptideAtlas; P03974; -.
DR   GeneID; 397524; -.
DR   KEGG; ssc:397524; -.
DR   CTD; 7415; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   InParanoid; P03974; -.
DR   OrthoDB; 168438at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR   GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
DR   GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR   GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR   GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR   GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
DR   GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR   GO; GO:0035617; P:stress granule disassembly; ISS:UniProtKB.
DR   GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR   CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 6.10.20.150; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005938; AAA_ATPase_CDC48.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01243; CDC48; 1.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF69; TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 2.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 2.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Autophagy; Cytoplasm; Direct protein sequencing;
KW   DNA damage; DNA repair; Endoplasmic reticulum; Hydrolase; Isopeptide bond;
KW   Lipid-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transport; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   CHAIN           2..806
FT                   /note="Transitional endoplasmic reticulum ATPase"
FT                   /id="PRO_0000084574"
FT   REGION          708..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..806
FT                   /note="Interaction with UBXN6"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        768..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         521..526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         315
FT                   /note="N6,N6,N6-trimethyllysine; by VCPKMT"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         502
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         505
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         668
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         668
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         702
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         754
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         770
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         805
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   CROSSLNK        8
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
SQ   SEQUENCE   806 AA;  89289 MW;  83B36B03DB7D9B35 CRC64;
     MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK
     GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVHLGDVI SIQPCPDVKY GKRIHVLPID
     DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT
     VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG
     ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
     IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF
     GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL
     QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG
     GLEDVKRELQ DLVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI
     SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
     INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN
     LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM
     EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG
     AGPSQGSGGG TGGSVYTEDN DDDLYG
//