TRI17_HUMAN
ID TRI17_HUMAN Reviewed; 477 AA.
AC Q9Y577; B4DVJ2; Q5VST8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM17;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 16;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM17 {ECO:0000305};
DE AltName: Full=Testis RING finger protein;
DE AltName: Full=Tripartite motif-containing protein 17;
GN Name=TRIM17; Synonyms=RBCC, RNF16, TERF;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=9792805; DOI=10.1006/bbrc.1998.9502;
RA Ogawa S., Goto W., Orimo A., Hosoi T., Ouchi Y., Muramatsu M., Inoue S.;
RT "Molecular cloning of a novel RING finger-B box-coiled coil (RBCC) protein,
RT terf, expressed in the testis.";
RL Biochem. Biophys. Res. Commun. 251:515-519(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AUTOUBIQUITINATION, AND INTERACTION WITH
RP TRIM44.
RX PubMed=19358823; DOI=10.1016/j.bbrc.2009.04.010;
RA Urano T., Usui T., Takeda S., Ikeda K., Okada A., Ishida Y., Iwayanagi T.,
RA Otomo J., Ouchi Y., Inoue S.;
RT "TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase.";
RL Biochem. Biophys. Res. Commun. 383:263-268(2009).
RN [6]
RP FUNCTION.
RX PubMed=22023800; DOI=10.1093/jb/mvr128;
RA Endo H., Ikeda K., Urano T., Horie-Inoue K., Inoue S.;
RT "Terf/TRIM17 stimulates degradation of kinetochore protein ZWINT and
RT regulates cell proliferation.";
RL J. Biochem. 151:139-144(2012).
RN [7]
RP FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1.
RX PubMed=27562068; DOI=10.1242/jcs.190017;
RA Mandell M.A., Jain A., Kumar S., Castleman M.J., Anwar T., Eskelinen E.L.,
RA Johansen T., Prekeris R., Deretic V.;
RT "TRIM17 contributes to autophagy of midbodies while actively sparing other
RT targets from degradation.";
RL J. Cell Sci. 129:3562-3573(2016).
RN [8]
RP FUNCTION, AND INTERACTION WITH TRIM28.
RX PubMed=30042493; DOI=10.1038/s41418-018-0169-5;
RA Lionnard L., Duc P., Brennan M.S., Kueh A.J., Pal M., Guardia F., Mojsa B.,
RA Damiano M.A., Mora S., Lassot I., Ravichandran R., Cochet C.,
RA Aouacheria A., Potts P.R., Herold M.J., Desagher S., Kucharczak J.;
RT "TRIM17 and TRIM28 antagonistically regulate the ubiquitination and anti-
RT apoptotic activity of BCL2A1.";
RL Cell Death Differ. 26:902-917(2019).
CC -!- FUNCTION: E3 ubiquitin ligase that plays important roles in the
CC regulation of neuronal apoptosis, selective autophagy or cell
CC proliferation (PubMed:22023800, PubMed:19358823, PubMed:27562068).
CC Stimulates the degradation of kinetochore ZW10 interacting protein
CC ZWINT in a proteasome-dependent manner, leading to negative regulation
CC of cell proliferation (PubMed:22023800). Inhibits autophagic
CC degradation of diverse known targets while contributing to autophagy of
CC midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17
CC assembles into complexes with the key autophagy regulator BECN1
CC (PubMed:27562068). Controls neuronal apoptosis by mediating
CC ubiquitination and degradation of MCL1 to initiate neuronal death. In
CC addition, regulates NFAT transcription factors NFATC3 and NFATC4
CC activities by preventing their nuclear localization, thus inhibiting
CC their transcriptional activities. Decreases TRIM41-mediated degradation
CC of ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in
CC neuronal cells (By similarity). Prevents the E3 ubiquitin-ligase
CC activity of TRIM28 and its interaction with anti-apoptotic BCL2A1,
CC blocking TRIM28 from ubiquitinating BCL2A1 (PubMed:19358823).
CC {ECO:0000250|UniProtKB:Q7TPM3, ECO:0000269|PubMed:19358823,
CC ECO:0000269|PubMed:22023800, ECO:0000269|PubMed:27562068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via coiled coil) with TRIM44 (via coiled coil)
CC (PubMed:19358823). Interacts with TRIM28; this interaction prevents
CC TRIM28 activity on BCL2A1 (PubMed:30042493). Interacts with TRIM41;
CC this interaction prevents TRIM41 activity on ZSCAN2 (By similarity).
CC Interacts with BECN1 (PubMed:27562068). Interacts with NFATC3 and
CC NFATC4; these interactions prevent NFATC3 and NFATC4 nuclear
CC localization (By similarity). {ECO:0000250|UniProtKB:Q7TPM3,
CC ECO:0000269|PubMed:19358823, ECO:0000269|PubMed:27562068,
CC ECO:0000269|PubMed:30042493}.
CC -!- INTERACTION:
CC Q9Y577; O14964: HGS; NbExp=6; IntAct=EBI-743894, EBI-740220;
CC Q9Y577; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-743894, EBI-16439278;
CC Q9Y577; Q9HCM9: TRIM39; NbExp=8; IntAct=EBI-743894, EBI-739510;
CC Q9Y577; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-743894, EBI-725997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27562068}. Lysosome
CC {ECO:0000269|PubMed:27562068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y577-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y577-2; Sequence=VSP_040994, VSP_040995;
CC -!- TISSUE SPECIFICITY: Almost exclusively in the testis.
CC {ECO:0000269|PubMed:19358823}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:19358823}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF156271; AAD40286.1; -; mRNA.
DR EMBL; AK301105; BAG62704.1; -; mRNA.
DR EMBL; AL670729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033788; AAH33788.1; -; mRNA.
DR CCDS; CCDS1571.1; -. [Q9Y577-1]
DR CCDS; CCDS44327.1; -. [Q9Y577-2]
DR RefSeq; NP_001020111.1; NM_001024940.2. [Q9Y577-1]
DR RefSeq; NP_001128327.1; NM_001134855.1. [Q9Y577-2]
DR RefSeq; NP_057186.1; NM_016102.3. [Q9Y577-1]
DR RefSeq; XP_006711842.1; XM_006711779.2. [Q9Y577-1]
DR RefSeq; XP_011542511.1; XM_011544209.2. [Q9Y577-1]
DR RefSeq; XP_011542512.1; XM_011544210.2. [Q9Y577-1]
DR AlphaFoldDB; Q9Y577; -.
DR SMR; Q9Y577; -.
DR BioGRID; 119314; 35.
DR IntAct; Q9Y577; 25.
DR STRING; 9606.ENSP00000355658; -.
DR iPTMnet; Q9Y577; -.
DR PhosphoSitePlus; Q9Y577; -.
DR BioMuta; TRIM17; -.
DR DMDM; 38605530; -.
DR MassIVE; Q9Y577; -.
DR MaxQB; Q9Y577; -.
DR PaxDb; Q9Y577; -.
DR PeptideAtlas; Q9Y577; -.
DR PRIDE; Q9Y577; -.
DR Antibodypedia; 20781; 170 antibodies from 24 providers.
DR DNASU; 51127; -.
DR Ensembl; ENST00000295033.7; ENSP00000295033.3; ENSG00000162931.12. [Q9Y577-1]
DR Ensembl; ENST00000366697.6; ENSP00000355658.2; ENSG00000162931.12. [Q9Y577-1]
DR Ensembl; ENST00000366698.7; ENSP00000355659.2; ENSG00000162931.12. [Q9Y577-1]
DR Ensembl; ENST00000456946.6; ENSP00000403312.2; ENSG00000162931.12. [Q9Y577-2]
DR Ensembl; ENST00000645562.1; ENSP00000496098.1; ENSG00000285344.2. [Q9Y577-1]
DR Ensembl; ENST00000645958.1; ENSP00000495842.1; ENSG00000285344.2. [Q9Y577-1]
DR Ensembl; ENST00000646778.1; ENSP00000494586.1; ENSG00000285344.2. [Q9Y577-2]
DR Ensembl; ENST00000647385.2; ENSP00000493891.1; ENSG00000285344.2. [Q9Y577-1]
DR GeneID; 51127; -.
DR KEGG; hsa:51127; -.
DR MANE-Select; ENST00000366698.7; ENSP00000355659.2; NM_016102.4; NP_057186.1.
DR UCSC; uc001hsu.4; human. [Q9Y577-1]
DR CTD; 51127; -.
DR DisGeNET; 51127; -.
DR GeneCards; TRIM17; -.
DR HGNC; HGNC:13430; TRIM17.
DR HPA; ENSG00000162931; Tissue enriched (testis).
DR MIM; 606123; gene.
DR neXtProt; NX_Q9Y577; -.
DR OpenTargets; ENSG00000162931; -.
DR PharmGKB; PA37768; -.
DR VEuPathDB; HostDB:ENSG00000162931; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162155; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9Y577; -.
DR OMA; CAVGQKS; -.
DR PhylomeDB; Q9Y577; -.
DR TreeFam; TF338674; -.
DR PathwayCommons; Q9Y577; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9Y577; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51127; 13 hits in 1103 CRISPR screens.
DR GenomeRNAi; 51127; -.
DR Pharos; Q9Y577; Tbio.
DR PRO; PR:Q9Y577; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y577; protein.
DR Bgee; ENSG00000162931; Expressed in right hemisphere of cerebellum and 96 other tissues.
DR ExpressionAtlas; Q9Y577; baseline and differential.
DR Genevisible; Q9Y577; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR CDD; cd15812; SPRY_PRY_TRIM17; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR032918; TRIM17.
DR InterPro; IPR035687; TRIM17_PRY/SPRY.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103:SF397; PTHR24103:SF397; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Lysosome; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..477
FT /note="E3 ubiquitin-protein ligase TRIM17"
FT /id="PRO_0000056224"
FT DOMAIN 277..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..66
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 94..135
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 135..223
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 295..343
FT /note="EDVVPDATSAYPYLLLYESRQRRYLGSSPEGSGFCSKDRFVAYPCAVGQ ->
FT GKWAPRARTSDPGSLGDAPLYPLASEATNGGGSTSALPGDGHWLFTVPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040994"
FT VAR_SEQ 344..477
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040995"
SQ SEQUENCE 477 AA; 54418 MW; ECA4010661ADD28A CRC64;
MEAVELARKL QEEATCSICL DYFTDPVMTT CGHNFCRACI QLSWEKARGK KGRRKRKGSF
PCPECREMSP QRNLLPNRLL TKVAEMAQQH PGLQKQDLCQ EHHEPLKLFC QKDQSPICVV
CRESREHRLH RVLPAEEAVQ GYKLKLEEDM EYLREQITRT GNLQAREEQS LAEWQGKVKE
RRERIVLEFE KMNLYLVEEE QRLLQALETE EEETASRLRE SVACLDRQGH SLELLLLQLE
ERSTQGPLQM LQDMKEPLSR KNNVSVQCPE VAPPTRPRTV CRVPGQIEVL RGFLEDVVPD
ATSAYPYLLL YESRQRRYLG SSPEGSGFCS KDRFVAYPCA VGQTAFSSGR HYWEVGMNIT
GDALWALGVC RDNVSRKDRV PKCPENGFWV VQLSKGTKYL STFSALTPVM LMEPPSHMGI
FLDFEAGEVS FYSVSDGSHL HTYSQATFPG PLQPFFCLGA PKSGQMVIST VTMWVKG
