TTC7B_HUMAN
ID TTC7B_HUMAN Reviewed; 843 AA.
AC Q86TV6; Q86U24; Q86VT3;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Tetratricopeptide repeat protein 7B;
DE Short=TPR repeat protein 7B;
DE AltName: Full=Tetratricopeptide repeat protein 7-like-1;
DE Short=TPR repeat protein 7-like-1;
GN Name=TTC7B; Synonyms=TTC7L1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-843 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-843 (ISOFORMS 1 AND 2).
RC TISSUE=Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-843 (ISOFORM 1).
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE PI4K COMPLEX.
RX PubMed=23229899; DOI=10.1083/jcb.201206095;
RA Nakatsu F., Baskin J.M., Chung J., Tanner L.B., Shui G., Lee S.Y.,
RA Pirruccello M., Hao M., Ingolia N.T., Wenk M.R., De Camilli P.;
RT "PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its impact
RT on plasma membrane identity.";
RL J. Cell Biol. 199:1003-1016(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-673; SER-677;
RP SER-678 AND SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION IN THE PI4K COMPLEX.
RX PubMed=25608530; DOI=10.15252/embr.201439151;
RA Chung J., Nakatsu F., Baskin J.M., De Camilli P.;
RT "Plasticity of PI4KIIIalpha interactions at the plasma membrane.";
RL EMBO Rep. 16:312-320(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 8-750 IN COMPLEX WITH FAM126A,
RP FUNCTION, AND IDENTIFICATION IN THE PI4K COMPLEX.
RX PubMed=26571211; DOI=10.1038/ncb3271;
RA Baskin J.M., Wu X., Christiano R., Oh M.S., Schauder C.M., Gazzerro E.,
RA Messa M., Baldassari S., Assereto S., Biancheri R., Zara F., Minetti C.,
RA Raimondi A., Simons M., Walther T.C., Reinisch K.M., De Camilli P.;
RT "The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis
RT at the plasma membrane.";
RL Nat. Cell Biol. 18:132-138(2016).
CC -!- FUNCTION: Component of a complex required to localize
CC phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The
CC complex acts as a regulator of phosphatidylinositol 4-phosphate
CC (PtdIns(4)P) synthesis. In the complex, plays a central role in
CC bridging PI4KA to EFR3B and FAM126A, via direct interactions
CC (PubMed:26571211). {ECO:0000269|PubMed:23229899,
CC ECO:0000269|PubMed:26571211}.
CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
CC composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
CC FAM126 (FAM126A or FAM126B) (PubMed:23229899). Interacts with PI4KA,
CC interaction is direct (PubMed:26571211). Interacts with EFR3 (EFR3A or
CC EFR3B), interaction is direct (PubMed:26571211). Interacts with FAM126
CC (FAM126A or FAM126B), interaction is direct (PubMed:26571211).
CC Association with the PI4K complex is strongly reduced by TMEM150A
CC (PubMed:25608530). {ECO:0000269|PubMed:23229899,
CC ECO:0000269|PubMed:25608530, ECO:0000269|PubMed:26571211}.
CC -!- INTERACTION:
CC Q86TV6; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-12006098, EBI-3866319;
CC Q86TV6; Q9BYI3: FAM126A; NbExp=5; IntAct=EBI-12006098, EBI-11065686;
CC Q86TV6; Q8IXS8: FAM126B; NbExp=3; IntAct=EBI-12006098, EBI-8787606;
CC Q86TV6; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-12006098, EBI-743796;
CC Q86TV6; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-12006098, EBI-6257312;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23229899}.
CC Cell membrane {ECO:0000269|PubMed:23229899}. Note=Localizes to the
CC cytosol and is recruited to the plasma membrane following interaction
CC with EFR3 (EFR3A or EFR3B) (PubMed:23229899).
CC {ECO:0000269|PubMed:23229899}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86TV6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TV6-2; Sequence=VSP_008061;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI46128.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI46128.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL096869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL122020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL832848; CAI46128.1; ALT_SEQ; mRNA.
DR EMBL; BX247966; CAD62305.1; -; mRNA.
DR EMBL; BX248275; CAD62603.1; -; mRNA.
DR EMBL; BC048270; AAH48270.2; -; mRNA.
DR CCDS; CCDS32140.1; -. [Q86TV6-1]
DR RefSeq; NP_001010854.1; NM_001010854.1. [Q86TV6-1]
DR RefSeq; NP_001307350.1; NM_001320421.1.
DR RefSeq; XP_016876534.1; XM_017021045.1. [Q86TV6-2]
DR RefSeq; XP_016876535.1; XM_017021046.1.
DR PDB; 5DSE; X-ray; 2.90 A; A/C=7-843.
DR PDB; 6BQ1; EM; 3.60 A; B/F=1-843.
DR PDBsum; 5DSE; -.
DR PDBsum; 6BQ1; -.
DR AlphaFoldDB; Q86TV6; -.
DR SMR; Q86TV6; -.
DR BioGRID; 126922; 21.
DR CORUM; Q86TV6; -.
DR IntAct; Q86TV6; 8.
DR MINT; Q86TV6; -.
DR STRING; 9606.ENSP00000336127; -.
DR iPTMnet; Q86TV6; -.
DR PhosphoSitePlus; Q86TV6; -.
DR BioMuta; TTC7B; -.
DR DMDM; 226693616; -.
DR EPD; Q86TV6; -.
DR jPOST; Q86TV6; -.
DR MassIVE; Q86TV6; -.
DR MaxQB; Q86TV6; -.
DR PaxDb; Q86TV6; -.
DR PeptideAtlas; Q86TV6; -.
DR PRIDE; Q86TV6; -.
DR ProteomicsDB; 69737; -. [Q86TV6-1]
DR ProteomicsDB; 69738; -. [Q86TV6-2]
DR Antibodypedia; 26548; 24 antibodies from 13 providers.
DR DNASU; 145567; -.
DR Ensembl; ENST00000328459.11; ENSP00000336127.4; ENSG00000165914.15. [Q86TV6-1]
DR GeneID; 145567; -.
DR KEGG; hsa:145567; -.
DR MANE-Select; ENST00000328459.11; ENSP00000336127.4; NM_001010854.2; NP_001010854.1.
DR UCSC; uc001xyp.4; human. [Q86TV6-1]
DR CTD; 145567; -.
DR DisGeNET; 145567; -.
DR GeneCards; TTC7B; -.
DR HGNC; HGNC:19858; TTC7B.
DR HPA; ENSG00000165914; Low tissue specificity.
DR neXtProt; NX_Q86TV6; -.
DR OpenTargets; ENSG00000165914; -.
DR PharmGKB; PA134947112; -.
DR VEuPathDB; HostDB:ENSG00000165914; -.
DR eggNOG; KOG4162; Eukaryota.
DR GeneTree; ENSGT00940000158474; -.
DR HOGENOM; CLU_010512_1_0_1; -.
DR InParanoid; Q86TV6; -.
DR OMA; PRNEYEE; -.
DR OrthoDB; 167932at2759; -.
DR PhylomeDB; Q86TV6; -.
DR TreeFam; TF313783; -.
DR PathwayCommons; Q86TV6; -.
DR SignaLink; Q86TV6; -.
DR BioGRID-ORCS; 145567; 18 hits in 1078 CRISPR screens.
DR ChiTaRS; TTC7B; human.
DR GenomeRNAi; 145567; -.
DR Pharos; Q86TV6; Tbio.
DR PRO; PR:Q86TV6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86TV6; protein.
DR Bgee; ENSG00000165914; Expressed in lateral nuclear group of thalamus and 172 other tissues.
DR ExpressionAtlas; Q86TV6; baseline and differential.
DR Genevisible; Q86TV6; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR045819; TTC7_N.
DR Pfam; PF13181; TPR_8; 2.
DR Pfam; PF19440; TTC7_N; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..843
FT /note="Tetratricopeptide repeat protein 7B"
FT /id="PRO_0000106387"
FT REPEAT 97..131
FT /note="TPR 1"
FT REPEAT 219..252
FT /note="TPR 2"
FT REPEAT 363..396
FT /note="TPR 3"
FT REPEAT 397..430
FT /note="TPR 4"
FT REPEAT 479..514
FT /note="TPR 5"
FT REPEAT 516..548
FT /note="TPR 6"
FT REPEAT 549..582
FT /note="TPR 7"
FT REPEAT 696..729
FT /note="TPR 8"
FT REPEAT 730..763
FT /note="TPR 9"
FT REPEAT 765..797
FT /note="TPR 10"
FT REPEAT 798..831
FT /note="TPR 11"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q6P5"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q6P5"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q6P5"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q6P5"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 656
FT /note="G -> GNSPEAYFHGFPSLFSVS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008061"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 43..59
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 172..192
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 255..272
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:5DSE"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:5DSE"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 448..458
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 466..486
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 490..510
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 515..527
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 531..544
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 549..561
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 565..578
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 583..596
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 599..616
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 692..709
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 712..725
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 730..743
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 746..759
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 764..777
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 780..793
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 798..811
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 814..829
FT /evidence="ECO:0007829|PDB:5DSE"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:5DSE"
SQ SEQUENCE 843 AA; 94179 MW; ADAB8B36878AABDA CRC64;
MATKKAGSRL ETEIERCRSE CQWERIPELV KQLSAKLIAN DDMAELLLGE SKLEQYLKEH
PLRQGASPRG PKPQLTEVRK HLTAALDRGN LKSEFLQESN LIMAKLNYVE GDYKEALNIY
ARVGLDDLPL TAVPPYRLRV IAEAYATKGL CLEKLPISSS TSNLHVDREQ DVITCYEKAG
DIALLYLQEI ERVILSNIQN RSPKPGPAPH DQELGFFLET GLQRAHVLYF KNGNLTRGVG
RFRELLRAVE TRTTQNLRMT IARQLAEILL RGMCEQSYWN PLEDPPCQSP LDDPLRKGAN
TKTYTLTRRA RVYSGENIFC PQENTEEALL LLLISESMAN RDAVLSRIPE HKSDRLISLQ
SASVVYDLLT IALGRRGQYE MLSECLERAM KFAFEEFHLW YQFALSLMAA GKSARAVKVL
KECIRLKPDD ATIPLLAAKL CMGSLHWLEE AEKFAKTVVD VGEKTSEFKA KGYLALGLTY
SLQATDASLR GMQEVLQRKA LLAFQRAHSL SPTDHQAAFY LALQLAISRQ IPEALGYVRQ
ALQLQGDDAN SLHLLALLLS AQKHYHDALN IIDMALSEYP ENFILLFSKV KLQSLCRGPD
EALLTCKHML QIWKSCYNLT NPSDSGRGSS LLDRTIADRR QLNTITLPDF SDPETGSVHA
TSVAASRVEQ ALSEVASSLQ SSAPKQGPLH PWMTLAQIWL HAAEVYIGIG KPAEATACTQ
EAANLFPMSH NVLYMRGQIA ELRGSMDEAR RWYEEALAIS PTHVKSMQRL ALILHQLGRY
SLAEKILRDA VQVNSTAHEV WNGLGEVLQA QGNDAAATEC FLTALELEAS SPAVPFTIIP
RVL
