PSB7_MOUSE
ID PSB7_MOUSE Reviewed; 277 AA.
AC P70195; O09084; Q542F7; Q9CZH4; Q9DCF7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1;
DE AltName: Full=Macropain chain Z;
DE AltName: Full=Multicatalytic endopeptidase complex chain Z;
DE AltName: Full=Proteasome subunit Z;
DE Flags: Precursor;
GN Name=Psmb7; Synonyms=Mmc14;
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].
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=8799160; DOI=10.1073/pnas.93.17.9096;
RA Kasahara M., Hayashi M., Tanaka K., Inoko H., Sugaya K., Ikemura T.,
RA Ishibashi T.;
RT "Chromosomal localization of the proteasome Z subunit gene reveals an
RT ancient chromosomal duplication involving the major histocompatibility
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9096-9101(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Stohwasser R., Standera S., Peters I., Kloetzel P.-M., Groettrup M.;
RT "Molecular cloning of the mouse proteasome subunits MC14 and MECL-1:
RT reciprocally regulated tissue expression of interferon-gamma-modulated
RT proteasome subunits.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=9300697;
RA Hayashi M., Ishibashi T., Tanaka K., Kasahara M.;
RT "The mouse genes encoding the third pair of beta-type proteasome subunits
RT regulated reciprocally by IFN-gamma: structural comparison, chromosomal
RT localization, and analysis of the promoter.";
RL J. Immunol. 159:2760-2770(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic head, Heart, Testis, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [6]
RP PROTEIN SEQUENCE OF 226-237.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP FUNCTION.
RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA Sleckman B.P.;
RT "Proteasome activator PA200 is required for normal spermatogenesis.";
RL Mol. Cell. Biol. 26:2999-3007(2006).
RN [8]
RP INDUCTION BY DITHIOLETHIONE.
RX PubMed=17521679; DOI=10.1016/j.lfs.2007.04.014;
RA Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.;
RT "Tissue specific increase of the catalytic subunits of the 26S proteasome
RT by indirect antioxidant dithiolethione in mice: enhanced activity for
RT degradation of abnormal protein.";
RL Life Sci. 80:2411-2420(2007).
RN [9]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP AND FUNCTION.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a
CC trypsin-like activity. {ECO:0000269|PubMed:16581775,
CC ECO:0000269|PubMed:22341445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:Q99436};
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99436}. Nucleus
CC {ECO:0000250|UniProtKB:Q99436}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:Q99436}.
CC -!- INDUCTION: Up-regulated by the antioxidant dithiolethione (D3T) in
CC colon (at protein level). {ECO:0000269|PubMed:17521679}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; D83585; BAA12017.1; -; mRNA.
DR EMBL; Y10874; CAA71824.1; -; mRNA.
DR EMBL; D85570; BAA22857.1; -; Genomic_DNA.
DR EMBL; AK002823; BAB22385.1; -; mRNA.
DR EMBL; AK012613; BAB28354.1; -; mRNA.
DR EMBL; AK013961; BAB29085.1; -; mRNA.
DR EMBL; AK075759; BAC35937.1; -; mRNA.
DR EMBL; AK088276; BAC40251.1; -; mRNA.
DR EMBL; AK088765; BAC40556.1; -; mRNA.
DR EMBL; AK168823; BAE40650.1; -; mRNA.
DR EMBL; BC057662; AAH57662.1; -; mRNA.
DR CCDS; CCDS16010.1; -.
DR PIR; JC6122; JC6122.
DR RefSeq; NP_035317.1; NM_011187.1.
DR PDB; 3UNB; X-ray; 2.90 A; H/V/j/x=44-277.
DR PDB; 3UNE; X-ray; 3.20 A; H/V/j/x=44-277.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR AlphaFoldDB; P70195; -.
DR SMR; P70195; -.
DR BioGRID; 202424; 43.
DR CORUM; P70195; -.
DR IntAct; P70195; 4.
DR STRING; 10090.ENSMUSP00000028083; -.
DR MEROPS; T01.011; -.
DR iPTMnet; P70195; -.
DR PhosphoSitePlus; P70195; -.
DR SwissPalm; P70195; -.
DR REPRODUCTION-2DPAGE; IPI00136483; -.
DR REPRODUCTION-2DPAGE; P70195; -.
DR CPTAC; non-CPTAC-3735; -.
DR EPD; P70195; -.
DR jPOST; P70195; -.
DR MaxQB; P70195; -.
DR PaxDb; P70195; -.
DR PeptideAtlas; P70195; -.
DR PRIDE; P70195; -.
DR ProteomicsDB; 291763; -.
DR Antibodypedia; 30460; 330 antibodies from 33 providers.
DR DNASU; 19177; -.
DR Ensembl; ENSMUST00000028083; ENSMUSP00000028083; ENSMUSG00000026750.
DR GeneID; 19177; -.
DR KEGG; mmu:19177; -.
DR UCSC; uc008jnp.1; mouse.
DR CTD; 5695; -.
DR MGI; MGI:107637; Psmb7.
DR VEuPathDB; HostDB:ENSMUSG00000026750; -.
DR eggNOG; KOG0173; Eukaryota.
DR GeneTree; ENSGT00940000157419; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; P70195; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 977476at2759; -.
DR PhylomeDB; P70195; -.
DR TreeFam; TF106222; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19177; 29 hits in 67 CRISPR screens.
DR ChiTaRS; Psmb7; mouse.
DR PRO; PR:P70195; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P70195; protein.
DR Bgee; ENSMUSG00000026750; Expressed in medial ganglionic eminence and 257 other tissues.
DR Genevisible; P70195; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035216; Proteasome_beta7.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF42; PTHR11599:SF42; 1.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..43
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026647"
FT CHAIN 44..277
FT /note="Proteasome subunit beta type-7"
FT /id="PRO_0000026648"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 108
FT /note="L -> F (in Ref. 4; BAB28354)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="K -> E (in Ref. 4; BAB22385)"
FT /evidence="ECO:0000305"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 77..91
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 277 AA; 29891 MW; 3B8BA01B1E6392F2 CRC64;
MAAVSVFQPP VGGFSFDNCR RNAVLEADFA KKGFKLPKAR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LTTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPDME EEEAKKLVSE AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PFSVPNKKGT
RLGRYRCEKG TTAVLTEKVT PLEIEVLEET VQTMDTS
