AT8B3_HUMAN
ID AT8B3_HUMAN Reviewed; 1300 AA.
AC O60423; Q7Z485; Q8IVB8; Q8N4Y8; Q96M22;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Phospholipid-transporting ATPase IK {ECO:0000305};
DE EC=7.6.2.1;
DE AltName: Full=ATPase class I type 8B member 3;
GN Name=ATP8B3 {ECO:0000312|HGNC:HGNC:13535}; Synonyms=ATP1K, FOS37502_2;
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 3), AND TISSUE SPECIFICITY.
RX PubMed=12880872; DOI=10.1016/s1388-1981(03)00107-0;
RA Harris M.J., Arias I.M.;
RT "FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues
RT (ATP8B2 and ATP8B3) expressed throughout the body.";
RL Biochim. Biophys. Acta 1633:127-131(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-1300.
RC TISSUE=Testis;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=20947505; DOI=10.1074/jbc.m110.139006;
RA van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A.,
RA Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.;
RT "Heteromeric interactions required for abundance and subcellular
RT localization of human CDC50 proteins and class 1 P4-ATPases.";
RL J. Biol. Chem. 285:40088-40096(2010).
CC -!- FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP
CC coupled to the transport of aminophospholipids from the outer to the
CC inner leaflet of various membranes and ensures the maintenance of
CC asymmetric distribution of phospholipids. Phospholipid translocation
CC seems also to be implicated in vesicle formation and in uptake of lipid
CC signaling molecules. May be responsible for the maintenance of
CC asymmetric distribution of phosphatidylserine (PS) in spermatozoa
CC membranes. Involved in acrosome reactions and binding of spermatozoa to
CC zona pellucida. {ECO:0000250|UniProtKB:Q6UQ17}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:Q6UQ17};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q6UQ17};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:Q6UQ17};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000250|UniProtKB:Q6UQ17}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20947505}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O60423-2; Sequence=Displayed;
CC Name=2;
CC IsoId=O60423-1; Sequence=VSP_039716;
CC Name=3;
CC IsoId=O60423-3; Sequence=VSP_043554, VSP_043555, VSP_039716;
CC -!- TISSUE SPECIFICITY: Isoform 3 was only detected in testis.
CC {ECO:0000269|PubMed:12880872}.
CC -!- MISCELLANEOUS: Association with flippase complex beta subunits TMEM30A
CC and TMEM30A has not been detected, neither did their coexpression
CC change the localization in ER. {ECO:0000305|PubMed:20947505}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB71492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY302538; AAQ19028.1; -; mRNA.
DR EMBL; AC004755; AAC17601.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC012615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69455.1; -; Genomic_DNA.
DR EMBL; AK057452; BAB71492.1; ALT_INIT; mRNA.
DR EMBL; BC035162; AAH35162.3; -; mRNA.
DR CCDS; CCDS45901.1; -. [O60423-2]
DR CCDS; CCDS54196.1; -. [O60423-3]
DR RefSeq; NP_001171473.1; NM_001178002.2. [O60423-3]
DR RefSeq; NP_620168.1; NM_138813.3. [O60423-2]
DR RefSeq; XP_006722717.1; XM_006722654.2. [O60423-1]
DR RefSeq; XP_006722718.1; XM_006722655.2. [O60423-1]
DR AlphaFoldDB; O60423; -.
DR SMR; O60423; -.
DR BioGRID; 127132; 3.
DR ComplexPortal; CPX-6304; ATP8B3-CDC50A P4-ATPase complex.
DR IntAct; O60423; 1.
DR STRING; 9606.ENSP00000311336; -.
DR iPTMnet; O60423; -.
DR PhosphoSitePlus; O60423; -.
DR BioMuta; ATP8B3; -.
DR jPOST; O60423; -.
DR MassIVE; O60423; -.
DR PaxDb; O60423; -.
DR PeptideAtlas; O60423; -.
DR PRIDE; O60423; -.
DR ProteomicsDB; 49396; -. [O60423-2]
DR ProteomicsDB; 49397; -. [O60423-1]
DR ProteomicsDB; 49398; -. [O60423-3]
DR Antibodypedia; 67630; 55 antibodies from 11 providers.
DR DNASU; 148229; -.
DR Ensembl; ENST00000310127.10; ENSP00000311336.6; ENSG00000130270.16. [O60423-2]
DR Ensembl; ENST00000525591.5; ENSP00000437115.1; ENSG00000130270.16. [O60423-3]
DR GeneID; 148229; -.
DR KEGG; hsa:148229; -.
DR MANE-Select; ENST00000310127.10; ENSP00000311336.6; NM_138813.4; NP_620168.1.
DR UCSC; uc002ltv.5; human. [O60423-2]
DR CTD; 148229; -.
DR DisGeNET; 148229; -.
DR GeneCards; ATP8B3; -.
DR HGNC; HGNC:13535; ATP8B3.
DR HPA; ENSG00000130270; Group enriched (bone marrow, testis).
DR MIM; 605866; gene.
DR neXtProt; NX_O60423; -.
DR OpenTargets; ENSG00000130270; -.
DR PharmGKB; PA25168; -.
DR VEuPathDB; HostDB:ENSG00000130270; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000160463; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR InParanoid; O60423; -.
DR OMA; HNELTSH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; O60423; -.
DR TreeFam; TF300654; -.
DR PathwayCommons; O60423; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; O60423; -.
DR BioGRID-ORCS; 148229; 18 hits in 1078 CRISPR screens.
DR ChiTaRS; ATP8B3; human.
DR GeneWiki; ATP8B3; -.
DR GenomeRNAi; 148229; -.
DR Pharos; O60423; Tdark.
DR PRO; PR:O60423; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60423; protein.
DR Bgee; ENSG00000130270; Expressed in left testis and 104 other tissues.
DR ExpressionAtlas; O60423; baseline and differential.
DR Genevisible; O60423; HS.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030349; ATP8B3.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24092:SF78; PTHR24092:SF78; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Lipid transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1300
FT /note="Phospholipid-transporting ATPase IK"
FT /id="PRO_0000046367"
FT TOPO_DOM 1..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..177
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..430
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1028
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1029..1048
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1049..1078
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1101..1112
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1113..1135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1136..1141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1163..1182
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1183..1207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1208..1300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 939
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 943
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12880872"
FT /id="VSP_043554"
FT VAR_SEQ 354
FT /note="A -> ADGYMFV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12880872"
FT /id="VSP_043555"
FT VAR_SEQ 730
FT /note="Q -> QVYNEMEQDLR (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12880872"
FT /id="VSP_039716"
FT VARIANT 45
FT /note="G -> R (in dbSNP:rs7250872)"
FT /id="VAR_055544"
FT VARIANT 618
FT /note="V -> I (in dbSNP:rs8100856)"
FT /id="VAR_055545"
SQ SEQUENCE 1300 AA; 146752 MW; 356B1972DD49DFF5 CRC64;
MGTGPAQTPR STRAGPEPSP APPGPGDTGD SDVTQEGSGP AGIRGGETVI RAGMGDSPGR
GAPERRHKAQ PGRARKYEWR PEGPTSMGSL GQREDLQDED RNSAFTWKVQ ANNRAYNGQF
KEKVILCWQR KKYKTNVIRT AKYNFYSFLP LNLYEQFHRV SNLFFLIIII LQSIPDISTL
PWFSLSTPMV CLLFIRATRD LVDDMGRHKS DRAINNRPCQ ILMGKSFKQK KWQDLCVGDV
VCLRKDNIVP ADMLLLASTE PSSLCYVETV DIDGETNLKF RQALMVTHKE LATIKKMASF
QGTVTCEAPN SRMHHFVGCL EWNDKKYSLD IGNLLLRGCR IRNTDTCYGL VIYAGFDTKI
MKNCGKIHLK RTKLDLLMNK LVVVIFISVV LVCLVLAFGF GFSVKEFKDH HYYLSGVHGS
SVAAESFFVF WSFLILLSVT IPMSMFILSE FIYLGNSVFI DWDVQMYYKP QDVPAKARST
SLNDHLGQVE YIFSDKTGTL TQNILTFNKC CISGRVYGPD SEATTRPKEN PYLWNKFADG
KLLFHNAALL HLVRTNGDEA VREFWRLLAI CHTVMVRESP RERPDQLLYQ AASPDEGALV
TAARNFGYVF LSRTQDTVTI MELGEERVYQ VLAIMDFNST RKRMSVLVRK PEGAICLYTK
GADTVIFERL HRRGAMEFAT EEALAAFAQE TLRTLCLAYR EVAEDIYEDW QQRHQEASLL
LQNRAQALQQ LLGATAIEDR LQDGVPETIK CLKKSNIKIW VLTGDKQETA VNIGFACELL
SENMLILEEK EISRILETYW ENSNNLLTRE SLSQVKLALV INGDFLDKLL VSLRKEPRAL
AQNVNMDEAW QELGQSRRDF LYARRLSLLC RRFGLPLAAP PAQDSRARRS SEVLQERAFV
DLASKCQAVI CCRVTPKQKA LIVALVKKYH QVVTLAIGDG ANDINMIKTA DVGVGLAGQE
GMQAVQNSDF VLGQFCFLQR LLLVHGRWSY VRICKFLRYF FYKSMASMMV QVWFACYNGF
TGQPLYEGWF LALFNLLYST LPVLYIGLFE QDVSAEQSLE KPELYVVGQK DELFNYWVFV
QAIAHGVTTS LVNFFMTLWI SRDTAGPASF SDHQSFAVVV ALSCLLSITM EVILIIKYWT
ALCVATILLS LGFYAIMTTT TQSFWLFRVS PTTFPFLYAD LSVMSSPSIL LVVLLSVSIN
TFPVLALRVI FPALKELRAK EEKVEEGPSE EIFTMEPLPH VHRESRARRS SYAFSHREGY
ANLITQGTIL RRGPGVSSDI ASESLDPSDE EAASSPKESQ
