ID TBC9B_HUMAN Reviewed; 1250 AA.
AC Q66K14; D3DWQ5; D3DWQ6; O75163; Q53EY0; Q6MZI2; Q96H49;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=TBC1 domain family member 9B;
GN Name=TBC1D9B; Synonyms=KIAA0676;
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 MRNA], AND VARIANT THR-1119.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1250 (ISOFORM 2), AND VARIANT
RP THR-1119.
RC TISSUE=Brain, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 805-1250 (ISOFORM 2), AND VARIANT
RP THR-1119.
RC TISSUE=Colon;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1004-1250, AND VARIANT THR-1119.
RC TISSUE=Uterus;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-435, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-432 AND SER-435, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-432 AND SER-435, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-397; SER-435 AND SER-463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-1241, AND
RP IDENTIFICATION BY 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 [16]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-1086.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s).
CC -!- INTERACTION:
CC Q66K14-2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-10217736, EBI-720116;
CC Q66K14-2; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-10217736, EBI-739909;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66K14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66K14-2; Sequence=VSP_025699;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08919.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014576; BAA31651.1; -; mRNA.
DR EMBL; AC008393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53780.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53782.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53777.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53779.1; -; Genomic_DNA.
DR EMBL; BC008919; AAH08919.3; ALT_INIT; mRNA.
DR EMBL; BC080659; AAH80659.1; -; mRNA.
DR EMBL; AK223509; BAD97229.1; -; mRNA.
DR EMBL; BX641107; CAE46050.1; -; mRNA.
DR CCDS; CCDS43408.1; -. [Q66K14-1]
DR CCDS; CCDS4450.1; -. [Q66K14-2]
DR RefSeq; NP_055858.2; NM_015043.3. [Q66K14-2]
DR RefSeq; NP_942568.2; NM_198868.2. [Q66K14-1]
DR AlphaFoldDB; Q66K14; -.
DR SMR; Q66K14; -.
DR BioGRID; 116696; 100.
DR IntAct; Q66K14; 35.
DR MINT; Q66K14; -.
DR STRING; 9606.ENSP00000349291; -.
DR GlyGen; Q66K14; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q66K14; -.
DR PhosphoSitePlus; Q66K14; -.
DR BioMuta; TBC1D9B; -.
DR DMDM; 296452939; -.
DR EPD; Q66K14; -.
DR jPOST; Q66K14; -.
DR MassIVE; Q66K14; -.
DR MaxQB; Q66K14; -.
DR PaxDb; 9606-ENSP00000349291; -.
DR PeptideAtlas; Q66K14; -.
DR ProteomicsDB; 65950; -. [Q66K14-1]
DR ProteomicsDB; 65951; -. [Q66K14-2]
DR Pumba; Q66K14; -.
DR Antibodypedia; 50209; 79 antibodies from 14 providers.
DR DNASU; 23061; -.
DR Ensembl; ENST00000355235.8; ENSP00000347375.3; ENSG00000197226.13. [Q66K14-2]
DR Ensembl; ENST00000356834.7; ENSP00000349291.3; ENSG00000197226.13. [Q66K14-1]
DR Ensembl; ENST00000639361.2; ENSP00000491970.2; ENSG00000284400.2.
DR Ensembl; ENST00000639711.2; ENSP00000491373.2; ENSG00000284400.2.
DR GeneID; 23061; -.
DR KEGG; hsa:23061; -.
DR MANE-Select; ENST00000355235.8; ENSP00000347375.3; NM_015043.4; NP_055858.2. [Q66K14-2]
DR UCSC; uc003mlh.4; human. [Q66K14-1]
DR AGR; HGNC:29097; -.
DR CTD; 23061; -.
DR DisGeNET; 23061; -.
DR GeneCards; TBC1D9B; -.
DR HGNC; HGNC:29097; TBC1D9B.
DR HPA; ENSG00000197226; Low tissue specificity.
DR MIM; 618039; gene.
DR neXtProt; NX_Q66K14; -.
DR OpenTargets; ENSG00000197226; -.
DR PharmGKB; PA145148062; -.
DR VEuPathDB; HostDB:ENSG00000197226; -.
DR eggNOG; KOG4347; Eukaryota.
DR GeneTree; ENSGT00940000158554; -.
DR HOGENOM; CLU_003535_0_1_1; -.
DR InParanoid; Q66K14; -.
DR OMA; CTGEVPT; -.
DR OrthoDB; 3034081at2759; -.
DR PhylomeDB; Q66K14; -.
DR TreeFam; TF313145; -.
DR PathwayCommons; Q66K14; -.
DR SignaLink; Q66K14; -.
DR BioGRID-ORCS; 23061; 9 hits in 1062 CRISPR screens.
DR ChiTaRS; TBC1D9B; human.
DR GenomeRNAi; 23061; -.
DR Pharos; Q66K14; Tdark.
DR PRO; PR:Q66K14; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q66K14; Protein.
DR Bgee; ENSG00000197226; Expressed in right hemisphere of cerebellum and 115 other cell types or tissues.
DR ExpressionAtlas; Q66K14; baseline and differential.
DR Genevisible; Q66K14; HS.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR CDD; cd13351; PH-GRAM1_TCB1D9_TCB1D9B; 1.
DR CDD; cd13354; PH-GRAM2_TCB1D9_TCB1D9B; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR Gene3D; 1.10.10.750; Ypt/Rab-GAP domain of gyp1p, domain 1; 1.
DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR035969; Rab-GAP_TBC_sf.
DR InterPro; IPR036014; TCB1D9/TCB1D9B_PH-GRAM1.
DR InterPro; IPR036017; TCB1D9/TCB1D9B_PH-GRAM2.
DR PANTHER; PTHR47666; PROTEIN VASCULAR ASSOCIATED DEATH 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47666:SF3; TBC1 DOMAIN FAMILY MEMBER 9B; 1.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1250
FT /note="TBC1 domain family member 9B"
FT /id="PRO_0000288501"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 142..209
FT /note="GRAM 1"
FT DOMAIN 288..356
FT /note="GRAM 2"
FT DOMAIN 508..695
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 879..914
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 397..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 555
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 594
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 955..971
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_025699"
FT VARIANT 240
FT /note="L -> P (in dbSNP:rs1057078)"
FT /id="VAR_032440"
FT VARIANT 706
FT /note="V -> I (in dbSNP:rs10037618)"
FT /id="VAR_032441"
FT VARIANT 1086
FT /note="P -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036196"
FT VARIANT 1119
FT /note="K -> T (in dbSNP:rs30386)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9734811,
FT ECO:0000269|Ref.5"
FT /id="VAR_032442"
FT CONFLICT 893
FT /note="E -> G (in Ref. 5; BAD97229)"
FT /evidence="ECO:0000305"
FT CONFLICT 1231
FT /note="K -> R (in Ref. 6; CAE46050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1250 AA; 140525 MW; 35D9E4914B1D8311 CRC64;
MWLSPEEVLV ANALWVTERA NPFFVLQRRR GHGRGGGLTG LLVGTLDVVL DSSARVAPYR
ILHQTQDSQV YWTVACGSSR KEITKHWEWL ENNLLQTLSI FDSEEDITTF VKGKIHGIIA
EENKNLQPQG DEDPGKFKEA ELKMRKQFGM PEGEKLVNYY SCSYWKGRVP RQGWLYLTVN
HLCFYSFLLG KEVSLVVQWV DITRLEKNAT LLFPESIRVD TRDQELFFSM FLNIGETFKL
MEQLANLAMR QLLDSEGFLE DKALPRPIRP HRNISALKRD LDARAKNECY RATFRLPRDE
RLDGHTSCTL WTPFNKLHIP GQMFISNNYI CFASKEEDAC HLIIPLREVT IVEKADSSSV
LPSPLSISTK SKMTFLFANL KDRDFLVQRI SDFLQKTPSK QPGSIGSRKA SVVDPSTESS
PAPQEGSEQP ASPASPLSSR QSFCAQEAPT ASQGLLKLFQ KNSPMEDLGA KGAKEKMKEE
SWHIHFFEYG RGVCMYRTAK TRALVLKGIP ESLRGELWLL FSGAWNEMVT HPGYYAELVE
KSTGKYSLAT EEIERDLHRS MPEHPAFQNE LGIAALRRVL TAYAFRNPTI GYCQAMNIVT
SVLLLYGSEE EAFWLLVALC ERMLPDYYNT RVVGALVDQG IFEELTRDFL PQLSEKMQDL
GVISSISLSW FLTLFLSVMP FESAVVIVDC FFYEGIKVIL QVALAVLDAN MEQLLGCSDE
GEAMTMLGRY LDNVVNKQSV SPPIPHLRAL LSSSDDPPAE VDIFELLKVS YEKFSSLRAE
DIEQMRFKQR LKVIQSLEDT AKRSVVRAIP VDIGFSIEEL EDLYMVFKAK HLASQYWGCS
RTMAGRRDPS LPYLEQYRID ASQFRELFAS LTPWACGSHT PLLAGRMFRL LDENKDSLIN
FKEFVTGMSG MYHGDLTEKL KVLYKLHLPP ALSPEEAESA LEAAHYFTED SSSEASPLAS
DLDLFLPWEA QEALPQEEQE GSGSEERGEE KGTSSPDYRH YLRMWAKEKE AQKETIKDLP
KMNQEQFIEL CKTLYNMFSE DPMEQDLYHA IATVASLLLR IGEVGKKFSA RTGRKPRDCA
TEEDEPPAPE LHQDAARELQ PPAAGDPQAK AGGDTHLGKA PQESQVVVEG GSGEGQGSPS
QLLSDDETKD DMSMSSYSVV STGSLQCEDL ADDTVLVGGE ACSPTARIGG TVDTDWCISF
EQILASILTE SVLVNFFEKR VDIGLKIKDQ KKVERQFSTA SDHEQPGVSG
//
