ATG9B_HUMAN
ID ATG9B_HUMAN Reviewed; 924 AA.
AC Q674R7; A1A5D3; Q6JRW5; Q8N8I8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Autophagy-related protein 9B {ECO:0000305};
DE AltName: Full=APG9-like 2 {ECO:0000303|PubMed:15755735};
DE AltName: Full=Nitric oxide synthase 3-overlapping antisense gene protein {ECO:0000303|PubMed:15234981};
DE Short=Protein sONE {ECO:0000303|PubMed:15234981};
GN Name=ATG9B;
GN Synonyms=APG9L2 {ECO:0000303|PubMed:15755735},
GN NOS3AS {ECO:0000303|PubMed:15234981};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15234981; DOI=10.1074/jbc.m400271200;
RA Robb G.B., Carson A.R., Tai S.C., Fish J.E., Singh S., Yamada T.,
RA Scherer S.W., Nakabayashi K., Marsden P.A.;
RT "Post-transcriptional regulation of endothelial nitric-oxide synthase by an
RT overlapping antisense mRNA transcript.";
RL J. Biol. Chem. 279:37982-37996(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP IDENTIFICATION.
RX PubMed=15755735; DOI=10.1074/jbc.m413957200;
RA Yamada T., Carson A.R., Caniggia I., Umebayashi K., Yoshimori T.,
RA Nakabayashi K., Scherer S.W.;
RT "Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an
RT autophagy-related protein (APG9-like2) highly expressed in trophoblast.";
RL J. Biol. Chem. 280:18283-18290(2005).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=17403686; DOI=10.1074/jbc.m608318200;
RA Fish J.E., Matouk C.C., Yeboah E., Bevan S.C., Khan M., Patil K., Ohh M.,
RA Marsden P.A.;
RT "Hypoxia-inducible expression of a natural cis-antisense transcript
RT inhibits endothelial nitric-oxide synthase.";
RL J. Biol. Chem. 282:15652-15666(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18936157; DOI=10.1128/mcb.01082-08;
RA Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
RT "Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-
RT terminal domains using an Atg13-independent mechanism.";
RL Mol. Cell. Biol. 29:157-171(2009).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy by mediating
CC autophagosomal membrane expansion. Cycles between the preautophagosomal
CC structure/phagophore assembly site (PAS) and the cytoplasmic vesicle
CC pool and supplies membrane for the growing autophagosome. Lipid
CC scramblase activity plays a key role in preautophagosomal
CC structure/phagophore assembly by distributing the phospholipids that
CC arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the
CC luminal leaflet of the bilayer, thereby driving autophagosomal membrane
CC expansion (By similarity). In addition to autophagy, also plays a role
CC in necrotic cell death (By similarity). {ECO:0000250|UniProtKB:Q68FE2,
CC ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q7Z3C6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q7Z3C6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q7Z3C6};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- INTERACTION:
CC Q674R7-2; P49639: HOXA1; NbExp=3; IntAct=EBI-12837280, EBI-740785;
CC Q674R7-2; P32242: OTX1; NbExp=3; IntAct=EBI-12837280, EBI-740446;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:18936157}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18936157}. Note=Under amino acid starvation or
CC rapamycin treatment, redistributes from a juxtanuclear clustered pool
CC to a dispersed peripheral cytosolic pool (PubMed:18936157). The
CC starvation-induced redistribution depends on ULK1 and ATG13
CC (PubMed:18936157). {ECO:0000269|PubMed:18936157}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q674R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q674R7-2; Sequence=VSP_030410, VSP_030413;
CC Name=3;
CC IsoId=Q674R7-3; Sequence=VSP_030411, VSP_030412;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta (trophoblast cells)
CC and pituitary gland. Not expressed in vascular endothelial.
CC {ECO:0000269|PubMed:15234981}.
CC -!- INDUCTION: By hypoxia, leading to inhibit NOS3 expression.
CC {ECO:0000269|PubMed:17403686}.
CC -!- DOMAIN: Forms a homotrimer with a solvated central pore, which is
CC connected laterally to the cytosol through the cavity within each
CC protomer. Acts as a lipid scramblase that uses its central pore to
CC function: the central pore opens laterally to accommodate lipid
CC headgroups, thereby enabling lipid flipping and redistribution of
CC lipids added to the outer leaflet of ATG9B-containing vesicles, thereby
CC enabling growth into autophagosomes. {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- DOMAIN: The tyrosine-based sorting signal motif, also named YXX-psi
CC motif, promotes interaction with the AP-4 complex.
CC {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- MISCELLANEOUS: ATG9B gene is located on the opposite DNA strand of the
CC NOS3 gene at chromosome 7q36. The genes are oriented in a tail-to-tail
CC configuration and the mRNAs encoding ATG9B and NOS3 are complementary
CC for 662 nucleotides. ATG9B transcription may a role in NOS3
CC transcription regulation. {ECO:0000269|PubMed:15234981}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ86941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AC010973; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY515311; AAS87212.1; -; mRNA.
DR EMBL; AY316116; AAQ86941.1; ALT_INIT; mRNA.
DR EMBL; AK096734; BAC04853.1; -; mRNA.
DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128587; AAI28588.1; -; mRNA.
DR EMBL; BK004019; DAA05200.1; -; mRNA.
DR CCDS; CCDS83242.1; -. [Q674R7-1]
DR RefSeq; NP_001303985.1; NM_001317056.1. [Q674R7-1]
DR RefSeq; XP_011514367.1; XM_011516065.1.
DR RefSeq; XP_011514368.1; XM_011516066.2.
DR AlphaFoldDB; Q674R7; -.
DR SMR; Q674R7; -.
DR BioGRID; 130263; 21.
DR IntAct; Q674R7; 5.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR GlyGen; Q674R7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q674R7; -.
DR PhosphoSitePlus; Q674R7; -.
DR BioMuta; ATG9B; -.
DR DMDM; 74708555; -.
DR EPD; Q674R7; -.
DR jPOST; Q674R7; -.
DR MassIVE; Q674R7; -.
DR MaxQB; Q674R7; -.
DR PeptideAtlas; Q674R7; -.
DR PRIDE; Q674R7; -.
DR ProteomicsDB; 65973; -. [Q674R7-1]
DR ProteomicsDB; 65974; -. [Q674R7-2]
DR ProteomicsDB; 65975; -. [Q674R7-3]
DR Antibodypedia; 32933; 270 antibodies from 25 providers.
DR DNASU; 285973; -.
DR Ensembl; ENST00000469530.4; ENSP00000479879.1; ENSG00000181652.20. [Q674R7-1]
DR Ensembl; ENST00000605952.5; ENSP00000475737.2; ENSG00000181652.20. [Q674R7-1]
DR Ensembl; ENST00000639579.2; ENSP00000491504.1; ENSG00000181652.20. [Q674R7-1]
DR GeneID; 285973; -.
DR KEGG; hsa:285973; -.
DR MANE-Select; ENST00000639579.2; ENSP00000491504.1; NM_001317056.2; NP_001303985.1.
DR UCSC; uc064jfi.1; human. [Q674R7-1]
DR CTD; 285973; -.
DR DisGeNET; 285973; -.
DR GeneCards; ATG9B; -.
DR HGNC; HGNC:21899; ATG9B.
DR HPA; ENSG00000181652; Tissue enhanced (esophagus, skin).
DR MIM; 612205; gene.
DR neXtProt; NX_Q674R7; -.
DR OpenTargets; ENSG00000181652; -.
DR PharmGKB; PA134883165; -.
DR VEuPathDB; HostDB:ENSG00000181652; -.
DR GeneTree; ENSGT00390000014839; -.
DR HOGENOM; CLU_006200_2_0_1; -.
DR InParanoid; Q674R7; -.
DR OMA; PSHQCPQ; -.
DR OrthoDB; 712239at2759; -.
DR PhylomeDB; Q674R7; -.
DR PathwayCommons; Q674R7; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SignaLink; Q674R7; -.
DR BioGRID-ORCS; 285973; 8 hits in 206 CRISPR screens.
DR GenomeRNAi; 285973; -.
DR Pharos; Q674R7; Tbio.
DR PRO; PR:Q674R7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q674R7; protein.
DR Bgee; ENSG00000181652; Expressed in lower esophagus mucosa and 112 other tissues.
DR Genevisible; Q674R7; HS.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IDA:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISS:UniProtKB.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..924
FT /note="Autophagy-related protein 9B"
FT /id="PRO_0000314867"
FT TOPO_DOM 1..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..276
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 439..459
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 460..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..551
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 625..645
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 646..924
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 151..154
FT /note="Tyrosine-based sorting signal"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT COMPBIAS 26..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..514
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030410"
FT VAR_SEQ 322..340
FT /note="EELSSVPWAEVQSRLLALQ -> GKGREDTGMYWRGQPGGLD (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030411"
FT VAR_SEQ 341..924
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030412"
FT VAR_SEQ 515..572
FT /note="RTAAPPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVLAVEHVLTAMTALG
FT VTATVA -> MPSYPQPSVLRGSAPARCWSSSWSWLPASGWSNCFAQSATSSATGTSRC
FT FTGRPCTSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030413"
FT VARIANT 166
FT /note="P -> L (in dbSNP:rs61078191)"
FT /id="VAR_061030"
FT CONFLICT 12
FT /note="R -> K (in Ref. 2; BAC04853)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="S -> P (in Ref. 1; AAQ86941)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="T -> P (in Ref. 1; AAQ86941)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="T -> A (in Ref. 1; AAQ86941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 924 AA; 101019 MW; 80C242069DF3D91E CRC64;
MVSRMGWGGR RRRLGRWGDL GPGSVPLLPM PLPPPPPPSC RGPGGGRISI FSLSPAPHTR
SSPSSFSPPT AGPPCSVLQG TGASQSCHSA LPIPATPPTQ AQPAMTPASA SPSWGSHSTP
PLAPATPTPS QQCPQDSPGL RVGPLIPEQD YERLEDCDPE GSQDSPIHGE EQQPLLHVPE
GLRGSWHHIQ NLDSFFTKIY SYHQRNGFAC ILLEDVFQLG QFIFIVTFTT FLLRCVDYNV
LFANQPSNHT RPGPFHSKVT LSDAILPSAQ CAERIRSSPL LVLLLVLAAG FWLVQLLRSV
CNLFSYWDIQ VFYREALHIP PEELSSVPWA EVQSRLLALQ RSGGLCVQPR PLTELDIHHR
ILRYTNYQVA LANKGLLPAR CPLPWGGSAA FLSRGLALNV DLLLFRGPFS LFRGGWELPH
AYKRSDQRGA LAARWGRTVL LLAALNLALS PLVLAWQVLH VFYSHVELLR REPGALGARG
WSRLARLQLR HFNELPHELR ARLARAYRPA AAFLRTAAPP APLRTLLARQ LVFFAGALFA
ALLVLTVYDE DVLAVEHVLT AMTALGVTAT VARSFIPEEQ CQGRAPQLLL QTALAHMHYL
PEEPGPGGRD RAYRQMAQLL QYRAVSLLEE LLSPLLTPLF LLFWFRPRAL EIIDFFHHFT
VDVAGVGDIC SFALMDVKRH GHPQWLSAGQ TEASLSQRAE DGKTELSLMR FSLAHPLWRP
PGHSSKFLGH LWGRVQQDAA AWGATSARGP STPGVLSNCT SPLPEAFLAN LFVHPLLPPR
DLSPTAPCPA AATASLLASI SRIAQDPSSV SPGGTGGQKL AQLPELASAE MSLHVIYLHQ
LHQQQQQQEP WGEAAASILS RPCSSPSQPP SPDEEKPSWS SDGSSPASSP RQQWGTQKAR
NLFPGGFQVT TDTQKEPDRA SCTD
