ID   AT10A_MOUSE             Reviewed;        1508 AA.
AC   O54827; Q8R3B8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 4.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Phospholipid-transporting ATPase VA;
DE            EC=7.6.2.1 {ECO:0000250|UniProtKB:O60312};
DE   AltName: Full=ATPase class V type 10A;
DE   AltName: Full=P-locus fat-associated ATPase;
DE   AltName: Full=P4-ATPase flippase complex alpha subunit ATP10A;
GN   Name=Atp10a; Synonyms=Atpc5, Pfatp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=11015572; DOI=10.1152/physiolgenomics.1999.1.3.139;
RA   Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA   Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA   Williamson P.L., Schlegel R.A.;
RT   "Differential expression of putative transbilayer amphipath transporters.";
RL   Physiol. Genomics 1:139-150(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-435.
RX   PubMed=9548971; DOI=10.1101/gr.8.4.354;
RA   Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L.,
RA   Schlegel R.A.;
RT   "Multiple members of a third subfamily of P-type ATPases identified by
RT   genomic sequences and ESTs.";
RL   Genome Res. 8:354-361(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-1508.
RX   PubMed=12105293; DOI=10.1038/oby.2002.94;
RA   Dhar M., Hauser L., Johnson D.;
RT   "An aminophospholipid translocase associated with body fat and type 2
RT   diabetes phenotypes.";
RL   Obes. Res. 10:695-702(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 840-1508.
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   TISSUE SPECIFICITY.
RX   PubMed=11074018; DOI=10.1152/physiolgenomics.2000.4.1.93;
RA   Dhar M., Webb L.S., Smith L., Hauser L., Johnson D., West D.B.;
RT   "A novel ATPase on mouse chromosome 7 is a candidate gene for increased
RT   body fat.";
RL   Physiol. Genomics 4:93-100(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalytic component of P4-ATPase flippase complex, which
CC       catalyzes the hydrolysis of ATP coupled to the transport of
CC       phosphatidylcholine (PC) from the outer to the inner leaflet of the
CC       plasma membrane. Initiates inward plasma membrane bending and
CC       recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins
CC       involved in membrane tubulation and cell trafficking. Facilitates
CC       ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell
CC       spreading on extracellular matrix. Has low flippase activity toward
CC       glucosylceramide (GlcCer). {ECO:0000250|UniProtKB:O60312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000250|UniProtKB:O60312};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC         1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60312};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC         Evidence={ECO:0000250|UniProtKB:O60312};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP +
CC         H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O60312};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037;
CC         Evidence={ECO:0000250|UniProtKB:O60312};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
CC   -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC       catalytic alpha subunit ATP10A and an accessory beta subunit TMEM30A.
CC       {ECO:0000250|UniProtKB:O60312}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60312};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:O60312}. Endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:O60312}. Note=Exit from the
CC       endoplasmic reticulum requires the presence of TMEM30A, but not that of
CC       TMEM30B. {ECO:0000250|UniProtKB:O60312}.
CC   -!- TISSUE SPECIFICITY: Found in testis and in white adipose tissue. Also
CC       detected in fetal tissues. {ECO:0000269|PubMed:11074018}.
CC   -!- PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase
CC       signature sequence. {ECO:0000250|UniProtKB:O94823}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {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; AF156549; AAF09447.1; -; mRNA.
DR   EMBL; AF011337; AAC02902.1; -; mRNA.
DR   EMBL; AF372979; AAM20894.1; -; Genomic_DNA.
DR   EMBL; BC025643; AAH25643.1; -; mRNA.
DR   CCDS; CCDS39972.1; -.
DR   RefSeq; NP_033858.2; NM_009728.2.
DR   RefSeq; XP_006540643.1; XM_006540580.3.
DR   RefSeq; XP_006540644.1; XM_006540581.3.
DR   AlphaFoldDB; O54827; -.
DR   SMR; O54827; -.
DR   STRING; 10090.ENSMUSP00000129811; -.
DR   GlyGen; O54827; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O54827; -.
DR   PhosphoSitePlus; O54827; -.
DR   EPD; O54827; -.
DR   jPOST; O54827; -.
DR   PaxDb; 10090-ENSMUSP00000129811; -.
DR   PeptideAtlas; O54827; -.
DR   ProteomicsDB; 281865; -.
DR   Antibodypedia; 58541; 29 antibodies from 13 providers.
DR   DNASU; 11982; -.
DR   Ensembl; ENSMUST00000168747.3; ENSMUSP00000129811.2; ENSMUSG00000025324.9.
DR   GeneID; 11982; -.
DR   KEGG; mmu:11982; -.
DR   UCSC; uc009hef.2; mouse.
DR   AGR; MGI:1330809; -.
DR   CTD; 57194; -.
DR   MGI; MGI:1330809; Atp10a.
DR   VEuPathDB; HostDB:ENSMUSG00000025324; -.
DR   eggNOG; KOG0206; Eukaryota.
DR   GeneTree; ENSGT00940000157895; -.
DR   HOGENOM; CLU_000846_3_4_1; -.
DR   InParanoid; O54827; -.
DR   OMA; QALRCGR; -.
DR   OrthoDB; 275833at2759; -.
DR   PhylomeDB; O54827; -.
DR   TreeFam; TF354252; -.
DR   BRENDA; 7.6.2.1; 3474.
DR   Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 11982; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Atp10a; mouse.
DR   PRO; PR:O54827; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O54827; Protein.
DR   Bgee; ENSMUSG00000025324; Expressed in cumulus cell and 219 other cell types or tissues.
DR   ExpressionAtlas; O54827; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0140351; F:glycosylceramide flippase activity; ISO:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0140345; F:phosphatidylcholine flippase activity; ISS:UniProtKB.
DR   GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   GO; GO:1903527; P:positive regulation of membrane tubulation; ISS:UniProtKB.
DR   CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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   NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   Genevisible; O54827; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1508
FT                   /note="Phospholipid-transporting ATPase VA"
FT                   /id="PRO_0000046380"
FT   TOPO_DOM        1..79
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..107
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        336..366
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..1101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1102..1122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1123..1134
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1135..1154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1155..1184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1185..1206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1207..1213
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1214..1236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1237..1242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1243..1263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1264..1281
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1282..1306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1307..1508
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1334..1354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1407..1436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1481..1508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT   BINDING         431
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         431
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         432
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         433
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         433
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         715
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         757
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         781
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         824
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         904
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         905
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         906
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         1019
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         1025
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         1045
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT   BINDING         1048
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         1049
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         1049
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        16..22
FT                   /note="WRRPRRR -> KLAAAKK (in Ref. 2; AAC02902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        435
FT                   /note="T -> L (in Ref. 2; AAC02902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="I -> V (in Ref. 3; AAM20894)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        687
FT                   /note="E -> D (in Ref. 1; AAF09447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        840..842
FT                   /note="CWL -> TRP (in Ref. 4; AAH25643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        978
FT                   /note="T -> A (in Ref. 3; AAM20894)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1113
FT                   /note="F -> S (in Ref. 1; AAF09447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1434
FT                   /note="T -> S (in Ref. 1; AAF09447)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1508 AA;  168788 MW;  B542F86C9CD80E5B CRC64;
     MERELPAAEE SASSGWRRPR RRRWEGRTRT VRSNLLPPLG TEDSTIGAPK GERLLMRGCI
     QHLADNRLKT TKYTLLSFLP KNLFEQFHRL ANVYFVFIAL LNFVPAVNAF QPGLALAPVL
     FILAVTAIKD LWEDYSRHRS DHEINHLGCL VFSREEKKYV NRYWKEIRVG DFVRLCCNEI
     IPADILLLSS SDPDGLCHIE TANLDGETNL KRRQVVRGFS ELVSEFNPLT FTSVIECEKP
     NNDLSRFRGY IMHSNGEKAG LHKENLLLRG CTIRNTEAVA GIVIYAGHET KALLNNSGPR
     YKRSQLERQM NCDVLWCVLL LVCISLFSAV GHGLWVRRYQ EKKALFDVPE SDGSSLSPAT
     AAVYSFFTMI IVLQVLIPIS LYVSIEIVKV CQVYFINQDI ELYDEETDSQ LQCRALNITE
     DLGQIKYIFS DKTGTLTENK MVFRRCTVSG IEYSHDANAQ RLARYQEADS EEEEVVSKVG
     TISHRGSTGS HQSIWMTHKT QSIKSHRRTG SRAEAKRASM LSKHTAFSSP MEKDITPDPK
     LLEKVSECDR FLAIARHQEH PLAHLSPELS DVFDFFIALT ICNTVVVTSP DQPRQKVRVR
     FELKSPVKTI EDFLRRFTPS RLASGCSSIG NLSTSKSSHK SGSAFLPSLS QDSMLLGLEE
     KLGQTAPSIA SNGYASQAGQ EESWASECTT DQKCPGEQRE QQEGELRYEA ESPDEAALVY
     AARAYNCALV DRLHDQVSVE LPHLGRLTFE LLHTLGFDSI RKRMSVVIRH PLTDEINVYT
     KGADSVVMDL LLPCSSDDAR GRHQKKIRSK TQNYLNLYAV EGLRTLCIAK RVLSKEEYAC
     WLQSHIEAEA SVESREELLF QSAVRLETNL HLLGATGIED RLQEGVPETI AKLRQAGLQI
     WVLTGDKQET AINIAYACKL LDHGEEVITL NADSQEACAA LLDQCLSYVQ SRNPRSTLQN
     SESNLSVGFS FNPVSTSTDA SPSPSLVIDG RSLAYALEKS LEDKFLFLAK QCRSVLCCRS
     TPLQKSMVVK LVRSKLKAMT LAIGDGANDV SMIQVADVGV GISGQEGMQA VMASDFAVPR
     FRYLERLLIV HGHWCYSRLA NMVLYFFYKN TMFVGLLFWF QFYCGFSASA MIDQWYLIFF
     NLLFSSLPQL VTGVLDKDVP ADMLLREPQL YKSGQNMEEY RPRAFWLNMV DAAFQSLVCF
     FIPYLAYYDS DVDVFTWGTP VTAIALFTFL LHLGIETKTW TWLNWLACGF STFLFFSVAL
     IYNTSCATCY PPSNPYWTMQ TLLGDPLFYL TCLIAPIAAL LPRLFFKALQ GSLFPTQLQL
     GRQLAKKPLN KFSDPKETFA QGQPPGHSET ELSERKTMGP FETLPRDCAS QASQFTQQLT
     CSPEASGEPS AVDTNMPLRE NTLLEGLGSQ ASGSSMPRGA ISEVCPGDSK RQSTSASQTA
     RLSSLFHLPS FGSLNWISSL SLASGLGSVL QLSGSSLQMD KQDGEFLSNP PQPEQDLHSF
     QGQVTGYL
//