HTR5B_HUMAN
ID HTR5B_HUMAN Reviewed; 2071 AA.
AC Q9P2D3; B5MDU8; Q7Z3B2; Q9NVL7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=HEAT repeat-containing protein 5B;
GN Name=HEATR5B {ECO:0000312|HGNC:HGNC:29273};
GN Synonyms=KIAA1414 {ECO:0000312|HGNC:HGNC:29273},
GN p200 {ECO:0000312|HGNC:HGNC:29273}, p200a {ECO:0000312|HGNC:HGNC:29273};
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-2071 (ISOFORM 2).
RC TISSUE=Amygdala;
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 486-2071 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1399-2071 (ISOFORM 3).
RC TISSUE=Teratocarcinoma;
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 [5]
RP FUNCTION, SUBUNIT, IDENTIFICATION IN THE AFTIPHILIN-P200-GAMMA-SYNERGIN
RP COMPLEX, INTERACTION WITH AFTPH; SYNRG AND GGA1, AND SUBCELLULAR LOCATION.
RX PubMed=15758025; DOI=10.1091/mbc.e04-12-1077;
RA Hirst J., Borner G.H., Harbour M., Robinson M.S.;
RT "The aftiphilin/p200/gamma-synergin complex.";
RL Mol. Biol. Cell 16:2554-2565(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1737, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1563; SER-1564 AND SER-1737,
RP AND 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).
CC -!- FUNCTION: Component of clathrin-coated vesicles (PubMed:15758025).
CC Component of the aftiphilin/p200/gamma-synergin complex, which plays
CC roles in AP1G1/AP-1-mediated protein trafficking including the
CC trafficking of transferrin from early to recycling endosomes, and the
CC membrane trafficking of furin and the lysosomal enzyme cathepsin D
CC between the trans-Golgi network (TGN) and endosomes (PubMed:15758025).
CC {ECO:0000269|PubMed:15758025}.
CC -!- SUBUNIT: Self-associates (PubMed:15758025). Component of the
CC aftiphilin/p200/gamma-synergin complex, at least composed of
CC AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a
CC role in the AP1G1/AP-1-mediated protein trafficking from early to
CC recycling endosomes and between the trans-Golgi network (TGN) and
CC endosomes (PubMed:15758025). Within the complex interacts with
CC AFTPH/aftiphilin and SYNRG/gamma-synergin; the interactions are direct
CC (PubMed:15758025). Interacts with GGA1 (PubMed:15758025).
CC {ECO:0000269|PubMed:15758025}.
CC -!- INTERACTION:
CC Q9P2D3; Q12959: DLG1; NbExp=2; IntAct=EBI-2832021, EBI-357481;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:15758025}. Note=Localization at clathrin-
CC coated vesicles depends on AFTPH/aftiphilin.
CC {ECO:0000269|PubMed:15758025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P2D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2D3-2; Sequence=VSP_029690, VSP_029691;
CC Name=3;
CC IsoId=Q9P2D3-3; Sequence=VSP_029692;
CC -!- SIMILARITY: Belongs to the HEATR5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91733.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX538008; CAD97959.1; -; mRNA.
DR EMBL; AB037835; BAA92652.1; -; mRNA.
DR EMBL; AK001513; BAA91733.1; ALT_INIT; mRNA.
DR CCDS; CCDS33181.1; -. [Q9P2D3-1]
DR RefSeq; NP_061897.1; NM_019024.2. [Q9P2D3-1]
DR RefSeq; XP_011531236.1; XM_011532934.2. [Q9P2D3-1]
DR RefSeq; XP_016859867.1; XM_017004378.1. [Q9P2D3-3]
DR AlphaFoldDB; Q9P2D3; -.
DR BioGRID; 119993; 33.
DR IntAct; Q9P2D3; 12.
DR STRING; 9606.ENSP00000233099; -.
DR CarbonylDB; Q9P2D3; -.
DR iPTMnet; Q9P2D3; -.
DR PhosphoSitePlus; Q9P2D3; -.
DR SwissPalm; Q9P2D3; -.
DR BioMuta; HEATR5B; -.
DR DMDM; 162416219; -.
DR EPD; Q9P2D3; -.
DR jPOST; Q9P2D3; -.
DR MassIVE; Q9P2D3; -.
DR MaxQB; Q9P2D3; -.
DR PaxDb; Q9P2D3; -.
DR PeptideAtlas; Q9P2D3; -.
DR PRIDE; Q9P2D3; -.
DR ProteomicsDB; 83775; -. [Q9P2D3-1]
DR ProteomicsDB; 83776; -. [Q9P2D3-2]
DR ProteomicsDB; 83777; -. [Q9P2D3-3]
DR Antibodypedia; 52336; 19 antibodies from 8 providers.
DR DNASU; 54497; -.
DR Ensembl; ENST00000233099.6; ENSP00000233099.5; ENSG00000008869.12. [Q9P2D3-1]
DR GeneID; 54497; -.
DR KEGG; hsa:54497; -.
DR MANE-Select; ENST00000233099.6; ENSP00000233099.5; NM_019024.3; NP_061897.1.
DR UCSC; uc002rpp.2; human. [Q9P2D3-1]
DR CTD; 54497; -.
DR DisGeNET; 54497; -.
DR GeneCards; HEATR5B; -.
DR HGNC; HGNC:29273; HEATR5B.
DR HPA; ENSG00000008869; Low tissue specificity.
DR MIM; 619627; gene.
DR neXtProt; NX_Q9P2D3; -.
DR OpenTargets; ENSG00000008869; -.
DR PharmGKB; PA162390697; -.
DR VEuPathDB; HostDB:ENSG00000008869; -.
DR eggNOG; KOG1822; Eukaryota.
DR GeneTree; ENSGT00390000006205; -.
DR HOGENOM; CLU_000652_0_0_1; -.
DR InParanoid; Q9P2D3; -.
DR OMA; ADTHNEE; -.
DR OrthoDB; 71064at2759; -.
DR PhylomeDB; Q9P2D3; -.
DR TreeFam; TF300706; -.
DR PathwayCommons; Q9P2D3; -.
DR SignaLink; Q9P2D3; -.
DR BioGRID-ORCS; 54497; 24 hits in 1074 CRISPR screens.
DR ChiTaRS; HEATR5B; human.
DR GenomeRNAi; 54497; -.
DR Pharos; Q9P2D3; Tdark.
DR PRO; PR:Q9P2D3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9P2D3; protein.
DR Bgee; ENSG00000008869; Expressed in left ventricle myocardium and 192 other tissues.
DR ExpressionAtlas; Q9P2D3; baseline and differential.
DR Genevisible; Q9P2D3; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040108; Laa1/Sip1/HEATR5.
DR PANTHER; PTHR21663; PTHR21663; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..2071
FT /note="HEAT repeat-containing protein 5B"
FT /id="PRO_0000311994"
FT REPEAT 848..885
FT /note="HEAT 1"
FT REPEAT 1062..1099
FT /note="HEAT 2"
FT REPEAT 1290..1327
FT /note="HEAT 3"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1563
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 763..768
FT /note="RIPAGE -> LLFLVH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029690"
FT VAR_SEQ 769..2071
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029691"
FT VAR_SEQ 1684..1773
FT /note="NEDDMEKEACTVLGEGGDSGGLIPGKSLVFATMELLMFILVRHMPHLSTKVS
FT DSPSHIATKTRLSEESARLVAATVTILSDLPSLCSPAG -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029692"
FT VARIANT 1601
FT /note="S -> P (in dbSNP:rs2302657)"
FT /id="VAR_037392"
FT CONFLICT 324
FT /note="E -> G (in Ref. 2; CAD97959)"
FT /evidence="ECO:0000305"
FT CONFLICT 1640
FT /note="E -> G (in Ref. 4; BAA91733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2071 AA; 224302 MW; 5CAAD3A49BFC975E CRC64;
MELAHSLLLN EEALAQITEA KRPVFIFEWL RFLDKVLVAA NKTDVKEKQK KLVEQLTGLI
SSSPGPPTRK LLAKNLAALY SIGDTFTVFQ TLDKCNDIIR NKDDTAAYLP TKLAAVACVG
AFYEKMGRML GSAFPETVNN LLKSLKSAES QGRSEILMSL QKVLSGLGGA AASSHRDIYK
NARSLLTDRS MAVRCAVAKC LLELQNEAVF MWTAELENIA TLCFKALENS NYGVRVAVSK
LLGTVMATAL MPKQATVMRQ NVKRATFDEV LELMATGFLR GGSGFLKSGG EMLKVGGSVN
REVRVGVTQA YVVFVTTLGG QWLERSFATF LSHVLDLVSH PRATQTHVEA VYSRRCVSFI
LRATVGSLLG EKAQIAAAKE ICQAIGKQMK AVEAVVNDTS GENKSGAADI AASQHVMVCA
LQELGSLVQS LNATASPLIQ EASIGLLEIV TSVLLHPSMA ARLAAAWCLR CVAVALPFQL
TPFLDRCAER LNNLKTSPEA VSGYSFAMAA LLGGVHQCPL GIPHAKGKMV VSIAEDLLRT
AAQNSRLSLQ RTQAGWLLLG ALMTLGPSVV RYHLPKMLLL WRNVFPRSLK ELEAEKARGD
SFTWQVTLEG RAGALCAMRS FVAHCPELLT EDVIRKLMTP IECAMTMMSH IPSVMKAHGA
HLKASAAMVR LRLYDILALL PPKTYEGSFN ALLRELVAEF TLTDNSANTT TSLLRSLCHY
DDSVLLGSWL QETDHKSIED QLQPNSASGS GALEHDPSSI YLRIPAGEAV PGPLPLGVSV
IDASVALFGV VFPHVSYKHR LQMLDHFAEC VKQAKGVRQQ AVQLNIFTAV LSALKGLAEN
KSTLGPEEVR KSALTLVMGP LDNPNPILRC AAGEALGRMA QVVGEATFIA RMAQYSFDKL
KSARDVVSRT GHSLALGCLH RYVGGIGSGQ HLKTSVSILL ALAQDGTSPE VQTWSLHSLA
LIVDSSGPMY RGYVEPTLSL VLTLLLTVPP SHTEVHQCLG RCLGAIITTV GPELQGNGAT
TSTIRSSCLV GCAITQDHSD SLVQAAAISC LQQLHMFAPR HVNLSSLVPS LCVHLCSSHL
LLRRAAVACL RQLAQREAAE VCEYAMSLAK NTGDKESSSA NVSPFAPGVS SRTDIHCRHQ
GVNITETGLE GLLFGMLDRE TDRKLCSDIH DTLGHMLSSL AVEKLSHWLM LCKDVLAASS
DMSTATLLSS GKDEEAEKKD EMDDDTMFTT LGEEDKSKPF VAPRWATRVF AADCLCRIIN
LCENADQAHF DLALARSAKL RNPTNDLLVL HLSDLIRMAF MAATDHSNQL RMAGLQALED
IIKKFASVPE PEFPGHVILE QYQANVGAAL RPAFSQDTPS DIIAKACQVC STWIGSGVVS
DLNDLRRVHN LLVSSLDKVQ AGKGSSSQLY RESATTMEKL AVLKAWAEVY VVAMNIKKEA
ESKPKRAIKN TDDDDDDCGT IDELPPDSLI TLVQPELPTL SRLWLAALKD YALLTLPAEF
SSQLPPDGGA FYTPETIDTA RLHYRNSWAP ILHAVALWLN STGFTCSEST EAAAISGLQK
RSTSVNLNQA SGAVGSAKSL PEINKDRMHL ILGVSIQFLC SPRPEEPIEH VTACLQALHT
LLDSPYARVH IAEDQLIGVE LLSVLHRLLL TWNPSSVQLL VTGVVQQIVR AAQDYLQEKR
NTLNEDDMEK EACTVLGEGG DSGGLIPGKS LVFATMELLM FILVRHMPHL STKVSDSPSH
IATKTRLSEE SARLVAATVT ILSDLPSLCS PAGCMTILPT ILFLIARILK DTAIKSADNQ
VPPPVSAALQ GIKSIVTLSM AKTEAGVQKQ WTALIRSTLA CILEYSQPED SVPTPDEVSM
LTAIALFLWS ASNEIIGVQS LQNGCMNRFK NALNSCDPWV QAKCYQLLLS VFQHSNRALS
TPYIHSLAPI VVEKLKAVER NRPASNIELL AVQEGIKVLE TLVALGEEQN RVQLLALLVP
TLISYLLDEN SFASASSASK DLHEFALQNL MHIGPLYPHA FKTVMGAAPE LKVRLETAVR
ASQASKAKAA ARQPAPAIHS APTIKLKTSF F
