ID   POLH_MOUSE              Reviewed;         694 AA.
AC   Q9JJN0; Q9JJJ2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=DNA polymerase eta;
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:Q9Y253};
DE   AltName: Full=RAD30 homolog A;
DE   AltName: Full=Xeroderma pigmentosum variant type protein homolog;
GN   Name=Polh; Synonyms=Rad30a, Xpv;
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 [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv; TISSUE=Embryo;
RX   PubMed=10871396; DOI=10.1093/nar/28.13.2473;
RA   Yamada A., Masutani C., Iwai S., Hanaoka F.;
RT   "Complementation of defective translesion synthesis and UV light-
RT   sensitivity in xeroderma pigmentosum variant cells by human and mouse DNA
RT   polymerase eta.";
RL   Nucleic Acids Res. 28:2473-2480(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   INTERACTION WITH REV1.
RX   PubMed=14657033; DOI=10.1093/emboj/cdg626;
RA   Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K.,
RA   Kisker C., Friedberg E.C.;
RT   "Mouse Rev1 protein interacts with multiple DNA polymerases involved in
RT   translesion DNA synthesis.";
RL   EMBO J. 22:6621-6630(2003).
CC   -!- FUNCTION: DNA polymerase specifically involved in the DNA repair by
CC       translesion synthesis (TLS) (PubMed:10871396). Due to low processivity
CC       on both damaged and normal DNA, cooperates with the heterotetrameric
CC       (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA
CC       lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer
CC       is further extended by the tetrameric POLZ complex. In the case of 1,2-
CC       intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3'
CC       guanine (By similarity). Particularly important for the repair of UV-
CC       induced pyrimidine dimers (PubMed:10871396). Although inserts the
CC       correct base, may cause base transitions and transversions depending
CC       upon the context. May play a role in hypermutation at immunoglobulin
CC       genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic
CC       sites, but does not have any lyase activity, preventing the release of
CC       the 5'-deoxyribose phosphate (5'-dRP) residue. This covalent trapping
CC       of the enzyme by the 5'-dRP residue inhibits its DNA synthetic activity
CC       during base excision repair, thereby avoiding high incidence of
CC       mutagenesis. Targets POLI to replication foci (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y253, ECO:0000269|PubMed:10871396}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y253};
CC       Note=Binds 2 Mg(2+). Prefers Mg(2+), but can also use Mn(2+). In vitro,
CC       can also utilize other divalent cations such as Ca(2+).
CC       {ECO:0000250|UniProtKB:Q9Y253};
CC   -!- ACTIVITY REGULATION: The enzyme in complex with the DNA substrate binds
CC       a third divalent metal cation. The binding of this third divalent
CC       cation, which is coordinated by water molecules and two oxygen atoms
CC       from DNA and dNTP, is essential for catalyzing the DNA synthesis.
CC       {ECO:0000250|UniProtKB:Q9Y253}.
CC   -!- SUBUNIT: Interacts with REV1 (PubMed:14657033). Interacts with
CC       monoubiquitinated PCNA, but not unmodified PCNA (By similarity).
CC       Interacts with POLI; this interaction targets POLI to the replication
CC       machinery (By similarity). Interacts with PALB2 and BRCA2; the
CC       interactions are direct and are required to sustain the recruitment of
CC       POLH at blocked replication forks and to stimulate POLH-dependent DNA
CC       synthesis on D loop substrates (By similarity). Interacts (via C-
CC       terminus) with TRAIP. Interacts with ubiquitin (By similarity).
CC       Interacts with POLDIP2. {ECO:0000250|UniProtKB:Q9Y253,
CC       ECO:0000269|PubMed:14657033}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y253}.
CC       Note=Binding to ubiquitinated PCNA mediates colocalization to
CC       replication foci during DNA replication and persists at sites of
CC       stalled replication forks following UV irradiation. After UV
CC       irradiation, recruited to DNA damage sites within 1 hour, to a maximum
CC       of about 80%; this recruitment may not be not restricted to cells
CC       active in DNA replication. Colocalizes with TRAIP to nuclear foci.
CC       {ECO:0000250|UniProtKB:Q9Y253}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10871396}.
CC   -!- INDUCTION: Up-regulated in proliferating cultured fibroblasts.
CC       {ECO:0000269|PubMed:10871396}.
CC   -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC       subdomains, but the fingers and thumb subdomains are much smaller than
CC       in high-fidelity polymerases; residues from five sequence motifs of the
CC       Y-family cluster around an active site cleft that can accommodate DNA
CC       and nucleotide substrates with relaxed geometric constraints, with
CC       consequently higher rates of misincorporation and low processivity.
CC       {ECO:0000250|UniProtKB:Q9Y253}.
CC   -!- DOMAIN: The UBZ3-type zinc finger domain and the PIP-box mediate the
CC       interaction with ubiquitinated PCNA and are both necessary for the
CC       enzymatic activity in translesion synthesis.
CC       {ECO:0000250|UniProtKB:Q9Y253}.
CC   -!- PTM: Monoubiquitinated by RCHY1/PIRH2. Ubiquitination depends on
CC       integrity of the UBZ3-type zinc finger domain and is enhanced by TRAIP.
CC       Ubiquitination inhibits the ability of PolH to interact with PCNA and
CC       to bypass UV-induced lesions. {ECO:0000250|UniProtKB:Q9Y253}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; AB027128; BAA97570.1; -; mRNA.
DR   EMBL; AB037184; BAA97585.1; -; mRNA.
DR   EMBL; AK036296; BAC29375.1; -; mRNA.
DR   CCDS; CCDS28822.1; -.
DR   RefSeq; NP_109640.1; NM_030715.3.
DR   AlphaFoldDB; Q9JJN0; -.
DR   SMR; Q9JJN0; -.
DR   BioGRID; 219842; 8.
DR   IntAct; Q9JJN0; 1.
DR   STRING; 10090.ENSMUSP00000024749; -.
DR   iPTMnet; Q9JJN0; -.
DR   PhosphoSitePlus; Q9JJN0; -.
DR   EPD; Q9JJN0; -.
DR   MaxQB; Q9JJN0; -.
DR   PaxDb; 10090-ENSMUSP00000024749; -.
DR   ProteomicsDB; 289780; -.
DR   Pumba; Q9JJN0; -.
DR   Antibodypedia; 1879; 222 antibodies from 30 providers.
DR   DNASU; 80905; -.
DR   Ensembl; ENSMUST00000024749.9; ENSMUSP00000024749.8; ENSMUSG00000023953.10.
DR   GeneID; 80905; -.
DR   KEGG; mmu:80905; -.
DR   UCSC; uc008crx.1; mouse.
DR   AGR; MGI:1891457; -.
DR   CTD; 5429; -.
DR   MGI; MGI:1891457; Polh.
DR   VEuPathDB; HostDB:ENSMUSG00000023953; -.
DR   eggNOG; KOG2095; Eukaryota.
DR   GeneTree; ENSGT00940000157048; -.
DR   HOGENOM; CLU_012348_7_2_1; -.
DR   InParanoid; Q9JJN0; -.
DR   OMA; QNHRVAK; -.
DR   OrthoDB; 118267at2759; -.
DR   PhylomeDB; Q9JJN0; -.
DR   TreeFam; TF103010; -.
DR   Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR   Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR   BioGRID-ORCS; 80905; 5 hits in 112 CRISPR screens.
DR   ChiTaRS; Polh; mouse.
DR   PRO; PR:Q9JJN0; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9JJN0; Protein.
DR   Bgee; ENSMUSG00000023953; Expressed in endothelial cell of lymphatic vessel and 221 other cell types or tissues.
DR   ExpressionAtlas; Q9JJN0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071494; P:cellular response to UV-C; IMP:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISO:MGI.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0006301; P:postreplication repair; IDA:MGI.
DR   GO; GO:0006290; P:pyrimidine dimer repair; IDA:MGI.
DR   GO; GO:0009314; P:response to radiation; IBA:GO_Central.
DR   GO; GO:0010225; P:response to UV-C; ISO:MGI.
DR   CDD; cd01702; PolY_Pol_eta; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR041298; UBZ3.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR   PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF21704; POLH-Rev1_HhH; 1.
DR   Pfam; PF18439; zf_UBZ; 1.
DR   PIRSF; PIRSF036603; DPol_eta; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50173; UMUC; 1.
DR   PROSITE; PS51907; ZF_UBZ3; 1.
DR   Genevisible; Q9JJN0; MM.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW   DNA-directed DNA polymerase; Isopeptide bond; Magnesium; Manganese;
KW   Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Schiff base; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..694
FT                   /note="DNA polymerase eta"
FT                   /id="PRO_0000173987"
FT   DOMAIN          9..258
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   ZN_FING         609..643
FT                   /note="UBZ3-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT   REGION          565..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           682..689
FT                   /note="PIP-box"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   COMPBIAS        579..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         61
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   BINDING         616
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT   BINDING         619
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT   BINDING         631
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT   BINDING         635
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01255"
FT   CROSSLNK        663
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   CROSSLNK        667
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   CROSSLNK        675
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
FT   CROSSLNK        690
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y253"
SQ   SEQUENCE   694 AA;  76167 MW;  727895AB5DB84BC8 CRC64;
     MAPGQNRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV SYEARAFGVT
     RNMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM EIMSYFAVIE RASIDEAYID
     LTSAVQERLQ KLQGQPISAD LLPSTYIEGL PRGPTVEETV QKEAIRKQGL LQWLDSLQSD
     DPTSPDLRLT VGAMIVEEMR AAIESKTGFQ CSAGISHNKV LAKLACGLNK PNRQTLVSHG
     SVPQLFSQMP IRKIRSLGGK LGASVIEVLG IEYMGDLTQF TESQLQSHFG EKNGSWLYAM
     CRGIEHDPVK PRQLPKTIGC SKNFPGKTAL ATREQVQWWL LQLALELEER LTKDRNDNDR
     VATQLVVSIR FQGDRRLSSL RRCCALPRYD AHKMSQDAFA AIRNCNTSGI QTEWSPPLTM
     LFLCATKFSA AAPPACTDIT AFLSSDSSCQ PKVPIASSET RTQGSGPAVP TSKEAATSLA
     SFFQKAAKKQ RMKETSFVPL NTATEKLSSK PSLVFQSSQT TGSQSFFKQK SLLLQHTQLS
     NSAAPDPPQA SPAAQPSCLP AECVDSGPDD GAVKPVSSKA VSTEMNVAGD SPNVLDSPAY
     NSQEVTQRAT EDQVLCEKCD SLVPVWDMPE HTDYHFALEL QKSFLQPCTS KPQAIPAVSP
     QGKRNPKSPS ASSSKRLRPH GMQTLESFFK PLTH
//