TBC8B_HUMAN
ID TBC8B_HUMAN Reviewed; 1120 AA.
AC Q0IIM8; B9A6K5; B9A6K6; Q5JRB7; Q6ZVX5; Q9NXE3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=TBC1 domain family member 8B;
GN Name=TBC1D8B;
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] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 806-1120 (ISOFORM 1).
RC TISSUE=Hepatoma, and Pulmonary artery;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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].
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 [6]
RP VARIANTS NPHS20 HIS-246 AND SER-291, CHARACTERIZATION OF VARIANTS NPHS20
RP HIS-246 AND SER-291, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING, AND INTERACTION WITH RAB11B.
RX PubMed=30661770; DOI=10.1016/j.ajhg.2018.12.016;
RA Dorval G., Kuzmuk V., Gribouval O., Welsh G.I., Bierzynska A., Schmitt A.,
RA Miserey-Lenkei S., Koziell A., Haq S., Benmerah A., Mollet G., Boyer O.,
RA Saleem M.A., Antignac C.;
RT "TBC1D8B Loss-of-Function Mutations Lead to X-Linked Nephrotic Syndrome via
RT Defective Trafficking Pathways.";
RL Am. J. Hum. Genet. 104:348-355(2019).
CC -!- FUNCTION: Involved in vesicular recycling, probably as a RAB11B GTPase-
CC activating protein. {ECO:0000269|PubMed:30661770}.
CC -!- SUBUNIT: Interacts (via domain Rab-GAP TBC) with RAB11B (in GTP-bound
CC form). {ECO:0000269|PubMed:30661770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30661770}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0IIM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0IIM8-2; Sequence=VSP_033953, VSP_033954;
CC Name=3;
CC IsoId=Q0IIM8-3; Sequence=VSP_043710, VSP_033954;
CC -!- TISSUE SPECIFICITY: Kidney (at protein level).
CC {ECO:0000269|PubMed:30661770}.
CC -!- DEVELOPMENTAL STAGE: Expressed in glomerular podocytes and tubules in
CC the fetal kidney (gestational age 25 weeks)(at protein level).
CC {ECO:0000269|PubMed:30661770}.
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|UniProtKB:Q96BZ9}.
CC -!- DISEASE: Nephrotic syndrome 20 (NPHS20) [MIM:301028]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS20 is an X-linked, steroid-resistant form with onset at birth or in
CC the first years of life in affected males. Death in childhood may occur
CC in absence of renal transplantation. Carrier females may be unaffected
CC or have a mild disease with proteinuria. {ECO:0000269|PubMed:30661770}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91071.1; Type=Erroneous initiation; Evidence={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; AB449890; BAH16633.1; -; mRNA.
DR EMBL; AB449891; BAH16634.1; -; mRNA.
DR EMBL; AK000305; BAA91071.1; ALT_INIT; mRNA.
DR EMBL; AK123957; BAC85735.1; -; mRNA.
DR EMBL; AL391315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC122564; AAI22565.1; -; mRNA.
DR CCDS; CCDS14522.1; -. [Q0IIM8-1]
DR CCDS; CCDS14523.1; -. [Q0IIM8-3]
DR RefSeq; NP_060222.2; NM_017752.2. [Q0IIM8-1]
DR RefSeq; NP_942582.1; NM_198881.1. [Q0IIM8-3]
DR AlphaFoldDB; Q0IIM8; -.
DR SMR; Q0IIM8; -.
DR BioGRID; 120233; 6.
DR IntAct; Q0IIM8; 1.
DR STRING; 9606.ENSP00000349781; -.
DR iPTMnet; Q0IIM8; -.
DR PhosphoSitePlus; Q0IIM8; -.
DR BioMuta; TBC1D8B; -.
DR DMDM; 189029914; -.
DR EPD; Q0IIM8; -.
DR jPOST; Q0IIM8; -.
DR MassIVE; Q0IIM8; -.
DR MaxQB; Q0IIM8; -.
DR PaxDb; Q0IIM8; -.
DR PeptideAtlas; Q0IIM8; -.
DR PRIDE; Q0IIM8; -.
DR ProteomicsDB; 58757; -. [Q0IIM8-1]
DR ProteomicsDB; 58758; -. [Q0IIM8-2]
DR ProteomicsDB; 58759; -. [Q0IIM8-3]
DR Antibodypedia; 15056; 29 antibodies from 11 providers.
DR DNASU; 54885; -.
DR Ensembl; ENST00000310452.6; ENSP00000310675.2; ENSG00000133138.20. [Q0IIM8-3]
DR Ensembl; ENST00000357242.10; ENSP00000349781.5; ENSG00000133138.20. [Q0IIM8-1]
DR GeneID; 54885; -.
DR KEGG; hsa:54885; -.
DR MANE-Select; ENST00000357242.10; ENSP00000349781.5; NM_017752.3; NP_060222.2.
DR UCSC; uc004emn.5; human. [Q0IIM8-1]
DR CTD; 54885; -.
DR DisGeNET; 54885; -.
DR GeneCards; TBC1D8B; -.
DR HGNC; HGNC:24715; TBC1D8B.
DR HPA; ENSG00000133138; Low tissue specificity.
DR MalaCards; TBC1D8B; -.
DR MIM; 301027; gene.
DR MIM; 301028; phenotype.
DR neXtProt; NX_Q0IIM8; -.
DR OpenTargets; ENSG00000133138; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA145148061; -.
DR VEuPathDB; HostDB:ENSG00000133138; -.
DR eggNOG; KOG4347; Eukaryota.
DR GeneTree; ENSGT00940000159451; -.
DR HOGENOM; CLU_024152_0_0_1; -.
DR InParanoid; Q0IIM8; -.
DR OMA; GTKFAMW; -.
DR OrthoDB; 450360at2759; -.
DR PhylomeDB; Q0IIM8; -.
DR TreeFam; TF313145; -.
DR PathwayCommons; Q0IIM8; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q0IIM8; -.
DR BioGRID-ORCS; 54885; 11 hits in 700 CRISPR screens.
DR GenomeRNAi; 54885; -.
DR Pharos; Q0IIM8; Tdark.
DR PRO; PR:Q0IIM8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q0IIM8; protein.
DR Bgee; ENSG00000133138; Expressed in right adrenal gland cortex and 166 other tissues.
DR ExpressionAtlas; Q0IIM8; baseline and differential.
DR Genevisible; Q0IIM8; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR CDD; cd13350; PH-GRAM1_TBC1D8B; 1.
DR CDD; cd13352; PH-GRAM2_TBC1D8B; 1.
DR Gene3D; 2.30.29.30; -; 2.
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-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR036012; TBC1D8B_PH-GRAM1.
DR InterPro; IPR036015; TBC1D8B_PH-GRAM2.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; GTPase activation;
KW Reference proteome; Repeat.
FT CHAIN 1..1120
FT /note="TBC1 domain family member 8B"
FT /id="PRO_0000337183"
FT DOMAIN 145..212
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 285..353
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT DOMAIN 487..674
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 858..893
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1035..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 534
FT /note="Arginine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
FT SITE 573
FT /note="Glutamine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
FT VAR_SEQ 614..632
FT /note="ALVDQAVFEELIRDHLPQL -> SDDFMPLVRIQGQCVIG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_033953"
FT VAR_SEQ 614..632
FT /note="ALVDQAVFEELIRDHLPQL -> SDDFMPLVRIQGQCVIGEK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:19077034"
FT /id="VSP_043710"
FT VAR_SEQ 633..1120
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19077034"
FT /id="VSP_033954"
FT VARIANT 246
FT /note="Q -> H (in NPHS20; rescues only partially glomerular
FT filtration defects in tbc1d8b knockout fish; defective
FT vesicular trafficking in podocytes; dbSNP:rs761410195)"
FT /evidence="ECO:0000269|PubMed:15772651"
FT /id="VAR_082286"
FT VARIANT 291
FT /note="F -> S (in NPHS20; exhibits intracellular vesicular
FT localization; rescues only partially glomerular filtration
FT defects in tbc1d8b knockout fish; reduced podocyte
FT migration; defective vesicular trafficking in podocytes;
FT dbSNP:rs1602413491)"
FT /evidence="ECO:0000269|PubMed:15772651"
FT /id="VAR_082287"
FT CONFLICT 503
FT /note="A -> V (in Ref. 2; BAC85735)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="Y -> C (in Ref. 2; BAA91071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1120 AA; 128709 MW; 3629EF0AE95E7A96 CRC64;
MWLKPEEVLL KNALKLWLME RSNDYFVLQR RRGYGEEGGG GLTGLLVGTL DSVLDSTAKV
APFRILHQTP DSQVYLSIAC GANREEITKH WDWLEQNIMK TLSVFDSNED ITNFVQGKIR
GLIAEEGKHC FAKEDDPEKF REALLKFEKC FGLPEKEKLV TYYSCSYWKG RVPCQGWLYL
STNFLSFYSF LLGSEIKLII SWDEVSKLEK TSNVILTESI HVCSQGENHY FSMFLHINQT
YLLMEQLANY AIRRLFDKET FDNDPVLYNP LQITKRGLEN RAHSEQFNAF FRLPKGESLK
EVHECFLWVP FSHFNTHGKM CISENYICFA SQDGNQCSVI IPLREVLAID KTNDSSKSVI
ISIKGKTAFR FHEVKDFEQL VAKLRLRCGA ASTQYHDIST ELAISSESTE PSDNFEVQSL
TSQRECSKTV NTEALMTVFH PQNLETLNSK MLKEKMKEQS WKILFAECGR GVSMFRTKKT
RDLVVRGIPE TLRGELWMLF SGAVNDMATN PDYYTEVVEQ SLGTCNLATE EIERDLRRSL
PEHPAFQSDT GISALRRVLT AYAYRNPKIG YCQAMNILTS VLLLYAKEEE AFWLLVAVCE
RMLPDYFNRR IIGALVDQAV FEELIRDHLP QLTEHMTDMT FFSSVSLSWF LTLFISVLPI
ESAVNVVDCF FYDGIKAILQ LGLAILDYNL DKLLTCKDDA EAVTALNRFF DNVTNKDSPL
PSNVQQGSNV SDEKTSHTRV DITDLIRESN EKYGNIRYED IHSMRCRNRL YVIQTLEETT
KQNVLRVVSQ DVKLSLQELD ELYVIFKKEL FLSCYWCLGC PVLKHHDPSL PYLEQYQIDC
QQFRALYHLL SPWAHSANKD SLALWTFRLL DENSDCLINF KEFSSAIDIM YNGSFTEKLK
LLFKLHIPPA YTEVKSKDAS KGDELSKEEL LYFSQLHVSK PANEKEAESA KHSPEKGKGK
IDIQAYLSQW QDELFKKEEN IKDLPRMNQS QFIQFSKTLY NLFHEDPEEE SLYQAIAVVT
SLLLRMEEVG RKLHSPTSSA KGFSGTVCGS GGPSEEKTGS HLEKDPCSFR EEPQWSFAFE
QILASLLNEP ALVRFFEKPI DVKAKLENAR ISQLRSRTKM
