ABCA9_HUMAN
ID ABCA9_HUMAN Reviewed; 1624 AA.
AC Q8IUA7; Q6P655; Q8N2S4; Q8WWZ5; Q96MD8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ATP-binding cassette sub-family A member 9 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:12150964};
GN Name=ABCA9;
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), VARIANTS HIS-353 AND THR-1306, AND
RP TISSUE SPECIFICITY.
RA Arnould I., Schriml L.M., Prades C., Lachtermacher-Triunfol M.,
RA Schneider T., Maintoux C., Lemoine C., Debono D., Devaud C., Naudin L.,
RA Bauche S., Annat M., Annilo T., Allikmets R., Gold B., Denefle P.,
RA Rosier M., Dean M.;
RT "Identifying and characterizing a five-gene cluster of ATP-binding cassette
RT transporters mapping to human chromosome 17q24: a new subgroup within the
RT ABCA subfamily.";
RL GeneScreen 1:157-164(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), ALTERNATIVE SPLICING
RP (ISOFORMS 2; 3 AND 4), FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Macrophage;
RX PubMed=12150964; DOI=10.1016/s0006-291x(02)00659-9;
RA Piehler A., Kaminski W.E., Wenzel J.J., Langmann T., Schmitz G.;
RT "Molecular structure of a novel cholesterol-responsive A subclass ABC
RT transporter, ABCA9.";
RL Biochem. Biophys. Res. Commun. 295:408-416(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-856 (ISOFORM 1), AND VARIANT
RP HIS-353.
RC TISSUE=Embryo, and Small intestine;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-949.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: Transporter that may play a role in monocyte differentiation
CC and lipid transport and homeostasis. {ECO:0000305|PubMed:12150964}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IUA7-1; Sequence=Displayed;
CC Name=2; Synonyms=ABCA9delta+55;
CC IsoId=Q8IUA7-2; Sequence=VSP_020705;
CC Name=3; Synonyms=ABCA9delta+73;
CC IsoId=Q8IUA7-3; Sequence=VSP_020707, VSP_020709;
CC Name=4; Synonyms=ABCA9delta-95;
CC IsoId=Q8IUA7-4; Sequence=VSP_020708, VSP_020709;
CC Name=5;
CC IsoId=Q8IUA7-5; Sequence=VSP_020706;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in heart.
CC {ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues with higher expression
CC in fetal heart and kidney. {ECO:0000269|PubMed:12150964}.
CC -!- INDUCTION: Up-regulated during monocyte differentiation into
CC macrophages. Down-regulated by cholesterol loading of macrophages.
CC {ECO:0000269|PubMed:12150964}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62472.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11021.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AY028899; AAK30024.1; -; mRNA.
DR EMBL; AF423307; AAN32751.1; -; mRNA.
DR EMBL; AF423346; AAN32752.1; -; Genomic_DNA.
DR EMBL; AF423308; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423309; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423310; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423311; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423312; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423313; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423314; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423315; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423316; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423317; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423318; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423320; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423321; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423322; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423323; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423324; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423325; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423326; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423327; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423328; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423329; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423330; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423331; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423332; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423333; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423334; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423335; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423336; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423337; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423338; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423339; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423340; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423341; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423342; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423343; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423344; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; AF423345; AAN32752.1; JOINED; Genomic_DNA.
DR EMBL; BC062472; AAH62472.1; ALT_INIT; mRNA.
DR EMBL; AK057068; BAB71359.1; -; mRNA.
DR EMBL; AK074491; BAC11021.1; ALT_INIT; mRNA.
DR CCDS; CCDS11681.1; -. [Q8IUA7-1]
DR RefSeq; NP_525022.2; NM_080283.3. [Q8IUA7-1]
DR AlphaFoldDB; Q8IUA7; -.
DR SMR; Q8IUA7; -.
DR BioGRID; 115631; 7.
DR IntAct; Q8IUA7; 3.
DR STRING; 9606.ENSP00000342216; -.
DR TCDB; 3.A.1.211.16; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q8IUA7; 3 sites.
DR iPTMnet; Q8IUA7; -.
DR PhosphoSitePlus; Q8IUA7; -.
DR BioMuta; ABCA9; -.
DR DMDM; 74762471; -.
DR jPOST; Q8IUA7; -.
DR MassIVE; Q8IUA7; -.
DR PaxDb; Q8IUA7; -.
DR PeptideAtlas; Q8IUA7; -.
DR PRIDE; Q8IUA7; -.
DR ProteomicsDB; 70529; -. [Q8IUA7-1]
DR ProteomicsDB; 70531; -. [Q8IUA7-3]
DR ProteomicsDB; 70532; -. [Q8IUA7-4]
DR Antibodypedia; 31822; 180 antibodies from 31 providers.
DR DNASU; 10350; -.
DR Ensembl; ENST00000340001.9; ENSP00000342216.3; ENSG00000154258.17. [Q8IUA7-1]
DR Ensembl; ENST00000495634.5; ENSP00000465601.1; ENSG00000154258.17. [Q8IUA7-5]
DR GeneID; 10350; -.
DR KEGG; hsa:10350; -.
DR MANE-Select; ENST00000340001.9; ENSP00000342216.3; NM_080283.4; NP_525022.2.
DR UCSC; uc002jhu.4; human. [Q8IUA7-1]
DR CTD; 10350; -.
DR DisGeNET; 10350; -.
DR GeneCards; ABCA9; -.
DR HGNC; HGNC:39; ABCA9.
DR HPA; ENSG00000154258; Low tissue specificity.
DR MIM; 612507; gene.
DR neXtProt; NX_Q8IUA7; -.
DR OpenTargets; ENSG00000154258; -.
DR PharmGKB; PA24384; -.
DR VEuPathDB; HostDB:ENSG00000154258; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162444; -.
DR HOGENOM; CLU_054320_0_0_1; -.
DR InParanoid; Q8IUA7; -.
DR OMA; YFEEHTS; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q8IUA7; -.
DR TreeFam; TF105192; -.
DR PathwayCommons; Q8IUA7; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR SignaLink; Q8IUA7; -.
DR BioGRID-ORCS; 10350; 6 hits in 1069 CRISPR screens.
DR ChiTaRS; ABCA9; human.
DR GeneWiki; ABCA9; -.
DR GenomeRNAi; 10350; -.
DR Pharos; Q8IUA7; Tbio.
DR PRO; PR:Q8IUA7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IUA7; protein.
DR Bgee; ENSG00000154258; Expressed in mucosa of stomach and 158 other tissues.
DR ExpressionAtlas; Q8IUA7; baseline and differential.
DR Genevisible; Q8IUA7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR030370; ABCA9.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF120; PTHR19229:SF120; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1624
FT /note="ATP-binding cassette sub-family A member 9"
FT /id="PRO_0000250680"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1065..1085
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1136..1156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1163..1183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1200..1220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 481..716
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1288..1521
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 517..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1326..1333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 267..1624
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020705"
FT VAR_SEQ 268..1624
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020706"
FT VAR_SEQ 1429
FT /note="L -> VRAGLVVALQVP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_020707"
FT VAR_SEQ 1429
FT /note="L -> AGDSGHL (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_020708"
FT VAR_SEQ 1430..1624
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_020709"
FT VARIANT 353
FT /note="R -> H (in dbSNP:rs1860447)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_027594"
FT VARIANT 785
FT /note="N -> S (in dbSNP:rs17684521)"
FT /id="VAR_027595"
FT VARIANT 1306
FT /note="K -> T (in dbSNP:rs2302294)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_027596"
FT VARIANT 1356
FT /note="G -> S (in dbSNP:rs9916254)"
FT /id="VAR_027597"
FT CONFLICT 1430
FT /note="C -> R (in Ref. 1; AAK30024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1624 AA; 184362 MW; 0847DC95DCC680D1 CRC64;
MSKRRMSVGQ QTWALLCKNC LKKWRMKRQT LLEWLFSFLL VLFLYLFFSN LHQVHDTPQM
SSMDLGRVDS FNDTNYVIAF APESKTTQEI MNKVASAPFL KGRTIMGWPD EKSMDELDLN
YSIDAVRVIF TDTFSYHLKF SWGHRIPMMK EHRDHSAHCQ AVNEKMKCEG SEFWEKGFVA
FQAAINAAII EIATNHSVME QLMSVTGVHM KILPFVAQGG VATDFFIFFC IISFSTFIYY
VSVNVTQERQ YITSLMTMMG LRESAFWLSW GLMYAGFILI MATLMALIVK SAQIVVLTGF
VMVFTLFLLY GLSLITLAFL MSVLIKKPFL TGLVVFLLIV FWGILGFPAL YTRLPAFLEW
TLCLLSPFAF TVGMAQLIHL DYDVNSNAHL DSSQNPYLII ATLFMLVFDT LLYLVLTLYF
DKILPAEYGH RCSPLFFLKS CFWFQHGRAN HVVLENETDS DPTPNDCFEP VSPEFCGKEA
IRIKNLKKEY AGKCERVEAL KGVVFDIYEG QITALLGHSG AGKTTLLNIL SGLSVPTSGS
VTVYNHTLSR MADIENISKF TGFCPQSNVQ FGFLTVKENL RLFAKIKGIL PHEVEKEVQR
VVQELEMENI QDILAQNLSG GQNRKLTFGI AILGDPQVLL LDEPTAGLDP LSRHRIWNLL
KEGKSDRVIL FSTQFIDEAD ILADRKVFIS NGKLKCAGSS LFLKKKWGIG YHLSLHLNER
CDPESITSLV KQHISDAKLT AQSEEKLVYI LPLERTNKFP ELYRDLDRCS NQGIEDYGVS
ITTLNEVFLK LEGKSTIDES DIGIWGQLQT DGAKDIGSLV ELEQVLSSFH ETRKTISGVA
LWRQQVCAIA KVRFLKLKKE RKSLWTILLL FGISFIPQLL EHLFYESYQK SYPWELSPNT
YFLSPGQQPQ DPLTHLLVIN KTGSTIDNFL HSLRRQNIAI EVDAFGTRNG TDDPSYNGAI
IVSGDEKDHR FSIACNTKRL NCFPVLLDVI SNGLLGIFNS SEHIQTDRST FFEEHMDYEY
GYRSNTFFWI PMAASFTPYI AMSSIGDYKK KAHSQLRISG LYPSAYWFGQ ALVDVSLYFL
ILLLMQIMDY IFSPEEIIFI IQNLLIQILC SIGYVSSLVF LTYVISFIFR NGRKNSGIWS
FFFLIVVIFS IVATDLNEYG FLGLFFGTML IPPFTLIGSL FIFSEISPDS MDYLGASESE
IVYLALLIPY LHFLIFLFIL RCLEMNCRKK LMRKDPVFRI SPRSNAIFPN PEEPEGEEED
IQMERMRTVN AMAVRDFDET PVIIASCLRK EYAGKKKNCF SKRKKKIATR NVSFCVKKGE
VIGLLGHNGA GKSTTIKMIT GDTKPTAGQV ILKGSGGGEP LGFLGYCPQE NALWPNLTVR
QHLEVYAAVK GLRKGDAMIA ITRLVDALKL QDQLKAPVKT LSEGIKRKLC FVLSILGNPS
VVLLDEPSTG MDPEGQQQMW QVIRATFRNT ERGALLTTHY MAEAEAVCDR VAIMVSGRLR
CIGSIQHLKS KFGKDYLLEM KLKNLAQMEP LHAEILRLFP QAAQQERFSS LMVYKLPVED
VRPLSQAFFK LEIVKQSFDL EEYSLSQSTL EQVFLELSKE QELGDLEEDF DPSVKWKLLL
QEEP
