TRI10_HUMAN
ID TRI10_HUMAN Reviewed; 481 AA.
AC Q9UDY6; A6NF84; Q5SRJ5; Q5SRK8; Q86Z08; Q96QB6; Q9C023; Q9C024;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Tripartite motif-containing protein 10;
DE AltName: Full=B30-RING finger protein;
DE AltName: Full=RING finger protein 9;
GN Name=TRIM10; Synonyms=RFB30, RNF9;
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 [GENOMIC DNA] (ISOFORM ALPHA).
RC TISSUE=Testis;
RX PubMed=9271628; DOI=10.1007/s002510050292;
RA Henry J., Ribouchon M.-T., Depetris D., Mattei M.-G., Offer C.,
RA Tazi-Ahnini R., Pontarotti P.;
RT "Cloning, structural analysis, and mapping of the B30 and B7 multigenic
RT families to the major histocompatibility complex (MHC) and other
RT chromosomal regions.";
RL Immunogenetics 46:383-395(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND SUBCELLULAR
RP LOCATION.
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Liver;
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 [9]
RP FUNCTION, INTERACTION WITH IFNAR1, AND SUBCELLULAR LOCATION.
RX PubMed=33811647; DOI=10.1002/eji.202049073;
RA Guo M., Cao W., Chen S., Tian R., Wang L., Liu Q., Zhang L., Wang Z.,
RA Zhao M., Lu Q., Zhu H.;
RT "TRIM10 binds to IFN-alpha/beta receptor 1 to negatively regulate type I
RT IFN signal transduction.";
RL Eur. J. Immunol. 51:1762-1773(2021).
CC -!- FUNCTION: E3 ligase that plays an essential role in the differentiation
CC and survival of terminal erythroid cells. May directly bind to PTEN and
CC promote its ubiquitination, resulting in its proteasomal degradation
CC and activation of hypertrophic signaling (By similarity). In addition,
CC plays a role in immune response regulation by repressing the
CC phosphorylation of STAT1 and STAT2 in the interferon/JAK/STAT signaling
CC pathway independent of its E3 ligase activity. Mechanistically,
CC interacts with the intracellular domain of IFNAR1 and thereby inhibits
CC the association between TYK2 and IFNAR1 (PubMed:33811647).
CC {ECO:0000250|UniProtKB:Q9WUH5, ECO:0000269|PubMed:33811647}.
CC -!- SUBUNIT: Interacts with IFNAR1; this interaction prevents association
CC of IFNAR1 with TYK2. {ECO:0000269|PubMed:33811647}.
CC -!- INTERACTION:
CC Q9UDY6; P25786: PSMA1; NbExp=4; IntAct=EBI-6427325, EBI-359352;
CC Q9UDY6; Q5W5X9: TTC23; NbExp=4; IntAct=EBI-6427325, EBI-6447954;
CC Q9UDY6; Q9UQR1: ZNF148; NbExp=3; IntAct=EBI-6427325, EBI-2688184;
CC Q9UDY6-2; P55040: GEM; NbExp=3; IntAct=EBI-11981577, EBI-744104;
CC Q9UDY6-2; O14964: HGS; NbExp=3; IntAct=EBI-11981577, EBI-740220;
CC Q9UDY6-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11981577, EBI-739832;
CC Q9UDY6-2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-11981577, EBI-748391;
CC Q9UDY6-2; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-11981577, EBI-17716262;
CC Q9UDY6-2; Q96DX7: TRIM44; NbExp=4; IntAct=EBI-11981577, EBI-8787399;
CC Q9UDY6-2; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-11981577, EBI-744257;
CC Q9UDY6-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-11981577, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331580,
CC ECO:0000269|PubMed:33811647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9UDY6-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9UDY6-2; Sequence=VSP_005748;
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y07829; CAB52384.1; -; Genomic_DNA.
DR EMBL; AF220122; AAG53495.1; -; mRNA.
DR EMBL; AF220123; AAG53496.1; -; mRNA.
DR EMBL; AB202085; BAE78605.1; -; Genomic_DNA.
DR EMBL; AB103595; BAF31256.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63332.1; -; Genomic_DNA.
DR EMBL; AB088089; BAC54921.1; -; Genomic_DNA.
DR EMBL; AL669914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR788282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03268.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03269.1; -; Genomic_DNA.
DR EMBL; BC093926; AAH93926.1; -; mRNA.
DR EMBL; BC113419; AAI13420.1; -; mRNA.
DR CCDS; CCDS34375.1; -. [Q9UDY6-1]
DR CCDS; CCDS4676.1; -. [Q9UDY6-2]
DR RefSeq; NP_006769.2; NM_006778.3. [Q9UDY6-1]
DR RefSeq; NP_439893.2; NM_052828.2. [Q9UDY6-2]
DR AlphaFoldDB; Q9UDY6; -.
DR SMR; Q9UDY6; -.
DR BioGRID; 115413; 51.
DR IntAct; Q9UDY6; 24.
DR STRING; 9606.ENSP00000397073; -.
DR PhosphoSitePlus; Q9UDY6; -.
DR BioMuta; TRIM10; -.
DR DMDM; 50403805; -.
DR EPD; Q9UDY6; -.
DR jPOST; Q9UDY6; -.
DR MassIVE; Q9UDY6; -.
DR PaxDb; Q9UDY6; -.
DR PeptideAtlas; Q9UDY6; -.
DR PRIDE; Q9UDY6; -.
DR ProteomicsDB; 84134; -. [Q9UDY6-1]
DR ProteomicsDB; 84135; -. [Q9UDY6-2]
DR Antibodypedia; 26232; 178 antibodies from 19 providers.
DR DNASU; 10107; -.
DR Ensembl; ENST00000259941.6; ENSP00000259941.6; ENSG00000137394.14. [Q9UDY6-2]
DR Ensembl; ENST00000354038.10; ENSP00000343695.6; ENSG00000137394.14. [Q9UDY6-1]
DR Ensembl; ENST00000376704.3; ENSP00000365894.3; ENSG00000204613.11. [Q9UDY6-2]
DR Ensembl; ENST00000413055.2; ENSP00000393787.2; ENSG00000227472.8. [Q9UDY6-2]
DR Ensembl; ENST00000416714.2; ENSP00000405578.2; ENSG00000229381.8. [Q9UDY6-2]
DR Ensembl; ENST00000417411.6; ENSP00000393576.2; ENSG00000237192.8. [Q9UDY6-2]
DR Ensembl; ENST00000426996.6; ENSP00000397440.2; ENSG00000227472.8. [Q9UDY6-1]
DR Ensembl; ENST00000428611.6; ENSP00000412370.2; ENSG00000229346.8. [Q9UDY6-2]
DR Ensembl; ENST00000431258.6; ENSP00000395598.2; ENSG00000235025.8. [Q9UDY6-1]
DR Ensembl; ENST00000446013.2; ENSP00000398404.2; ENSG00000237703.8. [Q9UDY6-2]
DR Ensembl; ENST00000447465.2; ENSP00000393976.2; ENSG00000235025.8. [Q9UDY6-2]
DR Ensembl; ENST00000448645.2; ENSP00000399446.2; ENSG00000229346.8. [Q9UDY6-1]
DR Ensembl; ENST00000449208.6; ENSP00000390497.2; ENSG00000237703.8. [Q9UDY6-1]
DR Ensembl; ENST00000449742.7; ENSP00000397073.2; ENSG00000204613.11. [Q9UDY6-1]
DR Ensembl; ENST00000451727.2; ENSP00000391445.2; ENSG00000237192.8. [Q9UDY6-1]
DR Ensembl; ENST00000456988.6; ENSP00000410849.2; ENSG00000229381.8. [Q9UDY6-1]
DR GeneID; 10107; -.
DR KEGG; hsa:10107; -.
DR MANE-Select; ENST00000449742.7; ENSP00000397073.2; NM_006778.4; NP_006769.2.
DR UCSC; uc003npn.3; human. [Q9UDY6-1]
DR CTD; 10107; -.
DR DisGeNET; 10107; -.
DR GeneCards; TRIM10; -.
DR HGNC; HGNC:10072; TRIM10.
DR HPA; ENSG00000204613; Tissue enhanced (bone marrow, kidney, liver).
DR MIM; 605701; gene.
DR neXtProt; NX_Q9UDY6; -.
DR OpenTargets; ENSG00000204613; -.
DR PharmGKB; PA35536; -.
DR VEuPathDB; HostDB:ENSG00000204613; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161525; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9UDY6; -.
DR OMA; SCTMGVV; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q9UDY6; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q9UDY6; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9UDY6; -.
DR BioGRID-ORCS; 10107; 11 hits in 1107 CRISPR screens.
DR ChiTaRS; TRIM10; human.
DR GenomeRNAi; 10107; -.
DR Pharos; Q9UDY6; Tbio.
DR PRO; PR:Q9UDY6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UDY6; protein.
DR Bgee; ENSG00000137394; Expressed in liver.
DR ExpressionAtlas; Q9UDY6; baseline and differential.
DR Genevisible; Q9UDY6; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd16593; RING-HC_TRIM10_C-IV; 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; IPR042784; TRIM10_RING-HC.
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 Pfam; PF13765; PRY; 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; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..481
FT /note="Tripartite motif-containing protein 10"
FT /id="PRO_0000056211"
FT DOMAIN 292..481
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..61
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 150..177
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 369..481
FT /note="VSIDLAHGGSCTVGVVSEDVQRKGELRLRPEEGVWAVRLAWGFVSALGSFPT
FT RLTLKEQPRQVRVSLDYEVGWVTFTNAVTREPIYTFTASFTRKVIPFFGLWGRGSSFSL
FT SS -> WMARVPGDSGCCQFCSPPSVLGTEVAA (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005748"
FT VARIANT 65
FT /note="R -> H (in dbSNP:rs12212092)"
FT /id="VAR_052127"
FT VARIANT 119
FT /note="V -> M (in dbSNP:rs17194446)"
FT /id="VAR_052128"
FT CONFLICT 104
FT /note="E -> G (in Ref. 1; CAB52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> SR (in Ref. 2; AAG53495/AAG53496)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="E -> K (in Ref. 2; AAG53495/AAG53496)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="Y -> S (in Ref. 1; CAB52384 and 2; AAG53495)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="G -> A (in Ref. 1; CAB52384 and 2; AAG53495)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9UDY6-2:379
FT /note="C -> G (in Ref. 2; AAG53496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 55037 MW; 49A1A11F391F5F98 CRC64;
MASAASVTSL ADEVNCPICQ GTLREPVTID CGHNFCRACL TRYCEIPGPD LEESPTCPLC
KEPFRPGSFR PNWQLANVVE NIERLQLVST LGLGEEDVCQ EHGEKIYFFC EDDEMQLCVV
CREAGEHATH TMRFLEDAAA PYREQIHKCL KCLRKEREEI QEIQSRENKR MQVLLTQVST
KRQQVISEFA HLRKFLEEQQ SILLAQLESQ DGDILRQRDE FDLLVAGEIC RFSALIEELE
EKNERPAREL LTDIRSTLIR CETRKCRKPV AVSPELGQRI RDFPQQALPL QREMKMFLEK
LCFELDYEPA HISLDPQTSH PKLLLSEDHQ RAQFSYKWQN SPDNPQRFDR ATCVLAHTGI
TGGRHTWVVS IDLAHGGSCT VGVVSEDVQR KGELRLRPEE GVWAVRLAWG FVSALGSFPT
RLTLKEQPRQ VRVSLDYEVG WVTFTNAVTR EPIYTFTASF TRKVIPFFGL WGRGSSFSLS
S
