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 28-JUN-2023, entry version 150. 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}; 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; 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. DR RefSeq; XP_016859867.1; XM_017004378.1. [Q9P2D3-3] DR AlphaFoldDB; Q9P2D3; -. DR BioGRID; 119993; 39. 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 ProteomicsDB; 83775; -. [Q9P2D3-1] DR ProteomicsDB; 83776; -. [Q9P2D3-2] DR ProteomicsDB; 83777; -. [Q9P2D3-3] DR Antibodypedia; 52336; 29 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 AGR; HGNC:29273; -. 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; HACILHI; -. DR OrthoDB; 1220778at2759; -. DR PhylomeDB; Q9P2D3; -. DR TreeFam; TF300706; -. DR PathwayCommons; Q9P2D3; -. DR SignaLink; Q9P2D3; -. DR BioGRID-ORCS; 54497; 25 hits in 1151 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; Leucine-rich Repeat Variant; 3. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR040108; Laa1/Sip1/HEATR5. DR InterPro; IPR046837; Laa1/Sip1/HEATR5-like_HEAT. DR PANTHER; PTHR21663:SF2; HEAT REPEAT-CONTAINING PROTEIN 5B; 1. DR PANTHER; PTHR21663; HYPOTHETICAL HEAT DOMAIN-CONTAINING; 1. DR Pfam; PF20210; Laa1_Sip1_HTR5; 1. DR SUPFAM; SSF48371; ARM repeat; 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 //