AT2B4_RAT
ID AT2B4_RAT Reviewed; 1203 AA.
AC Q64542; Q63127; Q63445; Q64543; Q64544; Q64545;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 4 {ECO:0000305};
DE Short=PMCA4 {ECO:0000303|PubMed:7702574, ECO:0000303|PubMed:7945253};
DE EC=7.2.2.10 {ECO:0000250|UniProtKB:P23634};
DE AltName: Full=Plasma membrane calcium ATPase isoform 4 {ECO:0000303|PubMed:7702574};
DE AltName: Full=Plasma membrane calcium pump isoform 4 {ECO:0000303|PubMed:7945253};
GN Name=Atp2b4 {ECO:0000312|RGD:621305};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XB; ZB; XA AND ZA), AND TISSUE
RP SPECIFICITY.
RC STRAIN=CD Charles River; TISSUE=Testis;
RX PubMed=7702574; DOI=10.1042/bj3060779;
RA Keeton T.P., Shull G.E.;
RT "Primary structure of rat plasma membrane Ca(2+)-ATPase isoform 4 and
RT analysis of alternative splicing patterns at splice site A.";
RL Biochem. J. 306:779-785(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 266-455 (ISOFORMS XA/XB).
RC TISSUE=Lung;
RX PubMed=7945253; DOI=10.1042/bj3030275;
RA Howard A., Barley N.F., Legon S., Walters J.R.F.;
RT "Plasma-membrane calcium-pump isoforms in human and rat liver.";
RL Biochem. J. 303:275-279(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1081-1203, ALTERNATIVE SPLICING
RP (ISOFORMS XA/ZA), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=8428948; DOI=10.1016/s0021-9258(18)53836-9;
RA Keeton T.P., Burk S.E., Shull G.E.;
RT "Alternative splicing of exons encoding the calmodulin-binding domains and
RT C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and 4.";
RL J. Biol. Chem. 268:2740-2748(1993).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-334; SER-1064 AND
RP SER-1070, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1115 AND SER-1126
RP (ISOFORM XA), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1103 AND
RP SER-1114 (ISOFORM ZA), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme
CC that catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium out of the cell (By similarity). By regulating sperm cell
CC calcium homeostasis, may play a role in sperm motility (By similarity).
CC {ECO:0000250|UniProtKB:P23634, ECO:0000250|UniProtKB:Q6Q477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000250|UniProtKB:P23634};
CC -!- ACTIVITY REGULATION: Activated by calcium/calmodulin.
CC {ECO:0000250|UniProtKB:P23634}.
CC -!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
CC Interacts with calmodulin. {ECO:0000250|UniProtKB:P23634}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23634};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium,
CC flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=There is a combination of two alternatively spliced domains
CC at N-terminal site A (X and Z) and at C-terminal site C (A and B).;
CC Name=XB; Synonyms=AIICI;
CC IsoId=Q64542-1; Sequence=Displayed;
CC Name=XA; Synonyms=AIICII;
CC IsoId=Q64542-2; Sequence=VSP_000407;
CC Name=ZA; Synonyms=AICII;
CC IsoId=Q64542-3; Sequence=VSP_000406, VSP_000407;
CC Name=ZB; Synonyms=AICI;
CC IsoId=Q64542-4; Sequence=VSP_000406;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Not detected in liver. The
CC highest levels are found in uterus and stomach. Isoform XA is found in
CC uterus, brain, stomach, small intestine, colon and pancreas. Isoform XB
CC is found in uterus, skeletal muscle, lung, kidney, spleen, stomach,
CC small intestine and pancreas. Isoform ZA is found in testis and isoform
CC ZB is found in testis and heart. {ECO:0000269|PubMed:7702574,
CC ECO:0000269|PubMed:8428948}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
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DR EMBL; U15408; AAA81005.1; -; mRNA.
DR EMBL; U15408; AAA81006.1; -; mRNA.
DR EMBL; U15408; AAA81007.1; -; mRNA.
DR EMBL; U15408; AAA81008.1; -; mRNA.
DR EMBL; X76452; CAA53990.1; -; mRNA.
DR EMBL; L05569; AAA50820.1; -; Genomic_DNA.
DR EMBL; L05566; AAA50820.1; JOINED; Genomic_DNA.
DR EMBL; L05567; AAA50820.1; JOINED; Genomic_DNA.
DR PIR; G44525; G44525.
DR PIR; S50027; S50027.
DR PIR; S54356; S54356.
DR PIR; S54357; S54357.
DR RefSeq; NP_001005871.1; NM_001005871.1. [Q64542-2]
DR RefSeq; XP_008767668.1; XM_008769446.2. [Q64542-1]
DR RefSeq; XP_008767669.1; XM_008769447.2. [Q64542-1]
DR RefSeq; XP_008767670.1; XM_008769448.2. [Q64542-4]
DR RefSeq; XP_008767671.1; XM_008769449.2. [Q64542-2]
DR RefSeq; XP_008767672.1; XM_008769450.2. [Q64542-3]
DR AlphaFoldDB; Q64542; -.
DR SMR; Q64542; -.
DR BioGRID; 248232; 2.
DR IntAct; Q64542; 2.
DR MINT; Q64542; -.
DR STRING; 10116.ENSRNOP00000004078; -.
DR iPTMnet; Q64542; -.
DR PhosphoSitePlus; Q64542; -.
DR jPOST; Q64542; -.
DR PaxDb; Q64542; -.
DR PRIDE; Q64542; -.
DR Ensembl; ENSRNOT00000004078; ENSRNOP00000004078; ENSRNOG00000003031. [Q64542-2]
DR Ensembl; ENSRNOT00000046273; ENSRNOP00000039880; ENSRNOG00000003031. [Q64542-1]
DR Ensembl; ENSRNOT00000112237; ENSRNOP00000080557; ENSRNOG00000003031. [Q64542-4]
DR GeneID; 29600; -.
DR KEGG; rno:29600; -.
DR UCSC; RGD:621305; rat. [Q64542-1]
DR CTD; 493; -.
DR RGD; 621305; Atp2b4.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000154527; -.
DR InParanoid; Q64542; -.
DR OMA; SKKYHEG; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q64542; -.
DR Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q64542; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003031; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q64542; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0097228; C:sperm principal piece; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:RGD.
DR GO; GO:0036487; F:nitric-oxide synthase inhibitor activity; ISO:RGD.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:1901660; P:calcium ion export; IMP:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:1905145; P:cellular response to acetylcholine; ISS:UniProtKB.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0140199; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:1900082; P:negative regulation of arginine catabolic process; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR GO; GO:1902548; P:negative regulation of cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:1903249; P:negative regulation of citrulline biosynthetic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:0098736; P:negative regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0003407; P:neural retina development; IEP:RGD.
DR GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051599; P:response to hydrostatic pressure; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR022141; ATP_Ca_trans_C.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Calmodulin-binding; Cell membrane; Cell projection; Cilium; Flagellum;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1203
FT /note="Plasma membrane calcium-transporting ATPase 4"
FT /id="PRO_0000046221"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..870
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 871..891
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 892..911
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..934
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 935..952
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 994..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1025
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1026..1047
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1048..1203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1103
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250|UniProtKB:P20020,
FT ECO:0000250|UniProtKB:P23634"
FT REGION 1104..1113
FT /note="Calmodulin-binding subdomain B"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23634"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1102
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Q477"
FT VAR_SEQ 301..312
FT /note="Missing (in isoform ZA and isoform ZB)"
FT /evidence="ECO:0000303|PubMed:7702574"
FT /id="VSP_000406"
FT VAR_SEQ 1105..1203
FT /note="RVVKVFHSFRDVIHKSKNQVSIHSFMTQPEYAADDEMSQSFLNQEESPSLAS
FT KSRITKRLSDAETVSQNNTNNNAVDCHQVQIVASHPNSPLQSQETPV -> EVINKFQT
FT GASFKGVLRRQNLSQQLDVKLVPSSYSEAVASVRTSPSTSSAVTPPPVGNQSGQSIS
FT (in isoform XA and isoform ZA)"
FT /evidence="ECO:0000303|PubMed:7702574"
FT /id="VSP_000407"
FT CONFLICT 431
FT /note="I -> V (in Ref. 2; CAA53990)"
FT /evidence="ECO:0000305"
FT MOD_RES Q64542-2:1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q64542-2:1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q64542-3:1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q64542-3:1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1203 AA; 133094 MW; B7A6C8D4556F6398 CRC64;
MTNPSGHNLP ANSVAESYEG EFGCTLMDLR KLMELRAADA VTQISAHYGS VQEICARLKT
SPVEGLSGNP ADLEKRRLVF GKNMIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
FYRPPGGENE ICGHIVSNPE EDEEGETGWI EGAAILASVI IVVFVTAFND WSKEKQFRGL
QSRIELEQKF SIIRNGQLIQ LPVAEIVVGD IAQVKYGDLL PADGILIQGN DLKIDESSLT
GESDHVKKTL DKDPMLLSGT HVMEGSGRMV VTAVGINSQT GIIFTLLGAN EEEDDEKKKK
GKKQGVSENR NKAKTQDGVA LEIQPLNSQE GLDSEEKEKK ASKGPKKEKS VLQGKLTRLA
VQIGKAGLIM SILTVLILIL YFVVDNFVIQ RRAWLPECTP VYIQYFVKFF IIGVTVLVVA
VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA
YIGGTHYRQI PKPDDLPPNV LDLIVNSICI NSAYTSKILP PEKEGGLPRQ VGNKTECGLL
GFVTDLKQDY QAVRSEMPEE KLFKVYTFNS VRKSMSTVIR KPEGGFRVFS KGASEIMLRK
CDRILNKEGG IVPFKTKDRD NMVRNVIEPM ASEGLRTIGI AYRDFDGEEP SWENENEIFT
GLVCIAVVGI EDPVRPEVPD AINKCKRAGI TVRMVTGDNV NTARAIATKC GILTPGDDFL
CLEGKEFNRL IRNEKGEVEQ EKLDKVWPRL RVLARSSPTD KHTLVKGIID SNIGEQRQVV
AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
SKFLQFQLTV NVVAVIVAFS GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTDSLL
RRRPYGRNKP LISRTMMKNI LGHAVYQLGI VFLLVFAGDK LFDIDSGRKA PLNSPPSQHY
TIVFNTFVLM QLFNEINSRK IHGEKNVFAG VYRNIIFCSV VLGTFFCQIL IVEVGGKPFS
CTNLTMEQWM WCLFIGIGEL LWGQVISAIP TKSLKFLKEA GHGSDKEEIS KDAEGLEEID
HAEMELRRGQ ILWVRGLNRI QTQIRVVKVF HSFRDVIHKS KNQVSIHSFM TQPEYAADDE
MSQSFLNQEE SPSLASKSRI TKRLSDAETV SQNNTNNNAV DCHQVQIVAS HPNSPLQSQE
TPV
