ID AUXI_BOVIN Reviewed; 910 AA.
AC Q27974;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Auxilin {ECO:0000303|PubMed:7705342};
DE EC=3.1.3.- {ECO:0000305};
DE AltName: Full=DnaJ homolog subfamily C member 6 {ECO:0000250|UniProtKB:O75061};
GN Name=DNAJC6 {ECO:0000250|UniProtKB:O75061};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE
RP SPECIFICITY, AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=7705342; DOI=10.1111/j.1432-1033.1995.tb20263.x;
RA Schroeder S., Morris S.A., Knorr R., Plessmann U., Weber K., Vinh N.G.,
RA Ungewickell E.;
RT "Primary structure of the neuronal clathrin-associated protein auxilin and
RT its expression in bacteria.";
RL Eur. J. Biochem. 228:297-304(1995).
RN [2]
RP FUNCTION, DOMAIN, AND INTERACTION WITH CLTC AND HSPA8.
RX PubMed=8524399; DOI=10.1038/378632a0;
RA Ungewickell E., Ungewickell H., Holstein S.E., Lindner R., Prasad K.,
RA Barouch W., Martin B., Greene L.E., Eisenberg E.;
RT "Role of auxilin in uncoating clathrin-coated vesicles.";
RL Nature 378:632-635(1995).
RN [3]
RP FUNCTION, AND INTERACTION WITH CLTC AND AP2A2.
RX PubMed=11470803; DOI=10.1074/jbc.m106511200;
RA Scheele U., Kalthoff C., Ungewickell E.;
RT "Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor
RT complex.";
RL J. Biol. Chem. 276:36131-36138(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH DNM1.
RX PubMed=12791276; DOI=10.1016/s1534-5807(03)00157-6;
RA Newmyer S.L., Christensen A., Sever S.;
RT "Auxilin-dynamin interactions link the uncoating ATPase chaperone machinery
RT with vesicle formation.";
RL Dev. Cell 4:929-940(2003).
RN [5]
RP FUNCTION.
RX PubMed=21482805; DOI=10.1073/pnas.1018845108;
RA Rothnie A., Clarke A.R., Kuzmic P., Cameron A., Smith C.J.;
RT "A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock
RT cognate protein (Hsc70) and auxilin.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6927-6932(2011).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=31962345; DOI=10.1083/jcb.201908142;
RA He K., Song E., Upadhyayula S., Dang S., Gaudin R., Skillern W., Bu K.,
RA Capraro B.R., Rapoport I., Kusters I., Ma M., Kirchhausen T.;
RT "Dynamics of Auxilin 1 and GAK in clathrin-mediated traffic.";
RL J. Cell Biol. 219:0-0(2020).
RN [7] {ECO:0007744|PDB:1NZ6}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 810-910, MUTAGENESIS OF LYS-847;
RP LYS-849 AND ASP-876, INTERACTION WITH HSPA8, AND DOMAIN.
RX PubMed=12741832; DOI=10.1021/bi034270g;
RA Jiang J., Taylor A.B., Prasad K., Ishikawa-Brush Y., Hart P.J., Lafer E.M.,
RA Sousa R.;
RT "Structure-function analysis of the auxilin J-domain reveals an extended
RT Hsc70 interaction interface.";
RL Biochemistry 42:5748-5753(2003).
RN [8] {ECO:0007744|PDB:1N4C}
RP STRUCTURE BY NMR OF 737-910, FUNCTION, AND SUBUNIT.
RX PubMed=15023062; DOI=10.1021/bi0354740;
RA Gruschus J.M., Han C.J., Greener T., Ferretti J.A., Greene L.E.,
RA Eisenberg E.;
RT "Structure of the functional fragment of auxilin required for catalytic
RT uncoating of clathrin-coated vesicles.";
RL Biochemistry 43:3111-3119(2004).
RN [9] {ECO:0007744|PDB:1XI5}
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 797-910 IN COMPLEX
RP WITH CLTC, AND FUNCTION.
RX PubMed=15502813; DOI=10.1038/nature03078;
RA Fotin A., Cheng Y., Grigorieff N., Walz T., Harrison S.C., Kirchhausen T.;
RT "Structure of an auxilin-bound clathrin coat and its implications for the
RT mechanism of uncoating.";
RL Nature 432:649-653(2004).
RN [10] {ECO:0007744|PDB:2QWN, ECO:0007744|PDB:2QWO, ECO:0007744|PDB:2QWP, ECO:0007744|PDB:2QWQ, ECO:0007744|PDB:2QWR}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 813-904 IN COMPLEX WITH HSPA8,
RP SUBUNIT, AND FUNCTION.
RX PubMed=17996706; DOI=10.1016/j.molcel.2007.08.022;
RA Jiang J., Maes E.G., Taylor A.B., Wang L., Hinck A.P., Lafer E.M.,
RA Sousa R.;
RT "Structural basis of J cochaperone binding and regulation of Hsp70.";
RL Mol. Cell 28:422-433(2007).
RN [11] {ECO:0007744|PDB:3N0A}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 40-400, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-301; ARG-307 AND LYS-311.
RX PubMed=20826345; DOI=10.1016/j.str.2010.06.016;
RA Guan R., Dai H., Harrison S.C., Kirchhausen T.;
RT "Structure of the PTEN-like region of auxilin, a detector of clathrin-
RT coated vesicle budding.";
RL Structure 18:1191-1198(2010).
CC -!- FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase
CC (Probable). Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated
CC vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin
CC from CCVs and participates in clathrin-mediated endocytosis of synaptic
CC vesicles and their recycling and also in intracellular trafficking
CC (PubMed:8524399, PubMed:11470803). Firstly, binds tightly to the
CC clathrin cages, at a ratio of one DNAJC6 per clathrin triskelion
CC (PubMed:21482805, PubMed:7705342, PubMed:15023062, PubMed:8524399,
CC PubMed:15502813). The HSPA8:ATP complex then binds to the clathrin-
CC auxilin cage, initially at a ratio of one HSPA8 per triskelion leading
CC to ATP hydrolysis stimulation and causing a conformational change in
CC the HSPA8 (PubMed:21482805, PubMed:15023062, PubMed:8524399,
CC PubMed:17996706). This cycle is repeated three times to drive to a
CC complex containing the clathrin-auxilin cage associated to three
CC HSPA8:ADP complex (PubMed:21482805). The ATP hydrolysis of the third
CC HSPA8:ATP complex leads to a concerted dismantling of the cage into
CC component triskelia (PubMed:21482805). Then, dissociates from the
CC released triskelia and be recycled to initiate another cycle of HSPA8's
CC recruitment (PubMed:21482805, PubMed:8524399). Also acts during the
CC early steps of clathrin-coated vesicle (CCV) formation through its
CC interaction with the GTP bound form of DNM1 (PubMed:12791276).
CC {ECO:0000269|PubMed:11470803, ECO:0000269|PubMed:12791276,
CC ECO:0000269|PubMed:15023062, ECO:0000269|PubMed:15502813,
CC ECO:0000269|PubMed:17996706, ECO:0000269|PubMed:21482805,
CC ECO:0000269|PubMed:7705342, ECO:0000269|PubMed:8524399, ECO:0000305}.
CC -!- SUBUNIT: Forms a complex composed of HSPA8, CLTC and DNAJC6
CC (PubMed:8524399). Interacts with HSPA8/HSC70 in an ATP-dependent
CC manner; this interaction stimulates the HSPA8's ATPase activity
CC (PubMed:12741832, PubMed:17996706). Interacts with CLTC; this
CC interaction produces a local change in heavy-chain contacts, creating a
CC detectable global distortion of the clathrin coat (PubMed:15502813,
CC PubMed:7705342, PubMed:15023062, PubMed:11470803). Interacts with AP2A2
CC (PubMed:11470803). Interacts with DNM1(GTP-bound form); this
CC interaction allows clathrin-coated vesicle (CCV) formation at the
CC plasma membrane (PubMed:12791276). {ECO:0000269|PubMed:11470803,
CC ECO:0000269|PubMed:12741832, ECO:0000269|PubMed:12791276,
CC ECO:0000269|PubMed:15023062, ECO:0000269|PubMed:15502813,
CC ECO:0000269|PubMed:17996706, ECO:0000269|PubMed:7705342,
CC ECO:0000269|PubMed:8524399}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:20826345, ECO:0000269|PubMed:31962345}.
CC Note=Appears on coated vesicles in successive transient bursts,
CC immediately after the vesicle release from the plasma membrane
CC (PubMed:31962345). Recruitment to clathrin-coated vesicles depends on
CC temporal variations in phosphoinositide composition of clathrin-coated
CC vesicles (PubMed:31962345). {ECO:0000269|PubMed:31962345}.
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:7705342}.
CC -!- DOMAIN: The J domain mediates interaction with HSPA8/HSC70
CC (PubMed:12741832) and is required for basket dissociation
CC (PubMed:8524399). {ECO:0000269|PubMed:12741832,
CC ECO:0000269|PubMed:8524399}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7705342}.
CC -!- PTM: Phosphorylation at Ser-567 modulates its ability to bind CLTC and
CC therefore the synaptic vesicle endocytosis (SVE).
CC {ECO:0000250|UniProtKB:O75061}.
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DR EMBL; U09237; AAA79037.1; -; mRNA.
DR PIR; S68983; S68983.
DR RefSeq; NP_777261.1; NM_174836.2.
DR PDB; 1N4C; NMR; -; A=737-910.
DR PDB; 1NZ6; X-ray; 2.50 A; A/B=810-910.
DR PDB; 1XI5; EM; 12.00 A; J/K/L/M/N/O/P/Q/R=797-910.
DR PDB; 2QWN; X-ray; 2.40 A; B=812-905.
DR PDB; 2QWO; X-ray; 1.70 A; B=813-904.
DR PDB; 2QWP; X-ray; 1.75 A; B=813-904.
DR PDB; 2QWQ; X-ray; 2.21 A; B=813-904.
DR PDB; 2QWR; X-ray; 2.21 A; B=813-904.
DR PDB; 3N0A; X-ray; 2.20 A; A=40-400.
DR PDBsum; 1N4C; -.
DR PDBsum; 1NZ6; -.
DR PDBsum; 1XI5; -.
DR PDBsum; 2QWN; -.
DR PDBsum; 2QWO; -.
DR PDBsum; 2QWP; -.
DR PDBsum; 2QWQ; -.
DR PDBsum; 2QWR; -.
DR PDBsum; 3N0A; -.
DR AlphaFoldDB; Q27974; -.
DR BMRB; Q27974; -.
DR EMDB; EMD-3442; -.
DR EMDB; EMD-4035; -.
DR EMDB; EMD-4036; -.
DR SMR; Q27974; -.
DR DIP; DIP-41952N; -.
DR ELM; Q27974; -.
DR IntAct; Q27974; 1.
DR MINT; Q27974; -.
DR STRING; 9913.ENSBTAP00000071020; -.
DR PaxDb; 9913-ENSBTAP00000041032; -.
DR GeneID; 317659; -.
DR KEGG; bta:317659; -.
DR CTD; 9829; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR InParanoid; Q27974; -.
DR EvolutionaryTrace; Q27974; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0072318; P:clathrin coat disassembly; IDA:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; ISS:UniProtKB.
DR GO; GO:1905443; P:regulation of clathrin coat assembly; ISS:UniProtKB.
DR GO; GO:0036465; P:synaptic vesicle recycling; ISS:UniProtKB.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd14563; PTP_auxilin_N; 1.
DR DisProt; DP00351; -.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR23172; AUXILIN/CYCLIN G-ASSOCIATED KINASE-RELATED; 1.
DR PANTHER; PTHR23172:SF4; TYROSINE-PROTEIN PHOSPHATASE AUXILIN-RELATED; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasmic vesicle; Direct protein sequencing;
KW Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW SH3-binding.
FT CHAIN 1..910
FT /note="Auxilin"
FT /id="PRO_0000215902"
FT REPEAT 33..36
FT /note="1"
FT REPEAT 37..40
FT /note="2"
FT REPEAT 41..44
FT /note="3"
FT DOMAIN 52..219
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 225..363
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 846..910
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 33..44
FT /note="3 X 4 AA approximate tandem repeats"
FT REGION 448..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 406..414
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 450..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75061"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ3"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ3"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75061"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75061"
FT MUTAGEN 301
FT /note="R->E: Impairs recruitment to the coated pits; when
FT associaited with E-307 and E-311."
FT /evidence="ECO:0000269|PubMed:20826345"
FT MUTAGEN 307
FT /note="R->E: Impairs recruitment to the coated pits; when
FT associaited with E-301 and E-311."
FT /evidence="ECO:0000269|PubMed:20826345"
FT MUTAGEN 311
FT /note="K->E: Impairs recruitment to the coated pits; when
FT associaited with E-301 and E-307."
FT /evidence="ECO:0000269|PubMed:20826345"
FT MUTAGEN 847
FT /note="K->C: Strongly reduces interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12741832"
FT MUTAGEN 849
FT /note="K->C: Slightly reduces interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12741832"
FT MUTAGEN 876
FT /note="D->A: Loss of interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12741832"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 291..304
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 310..323
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:1N4C"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:1N4C"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:1N4C"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:1N4C"
FT STRAND 786..789
FT /evidence="ECO:0007829|PDB:1N4C"
FT HELIX 801..809
FT /evidence="ECO:0007829|PDB:1N4C"
FT HELIX 814..826
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 830..836
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 837..839
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 853..855
FT /evidence="ECO:0007829|PDB:2QWO"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 859..872
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 875..878
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 884..903
FT /evidence="ECO:0007829|PDB:2QWO"
SQ SEQUENCE 910 AA; 99512 MW; BC156DC1CF3487FD CRC64;
MDSSGASSPD MEPSYGGGLF DMVKGGAGRL FSNLKDNLKD TLKDTSSRVI QSVTSYTKGD
LDFTYVTSRI IVMSFPLDSV DIGFRNQVDD IRSFLDSRHL DHYTVYNLSP KSYRTAKFHS
RVSECSWPIR QAPSLHNLFA VCRNMYNWLL QNPKNVCVVH CLDGRAASSI LVGAMFIFCN
LYSTPGPAVR LLYAKRPGIG LSPSHRRYLG YMCDLLADKP YRPHFKPLTI KSITVSPVPF
FNKQRNGCRP YCDVLIGETK IYTTCADFER MKEYRVQDGK IFIPLSITVQ GDVVVSMYHL
RSTIGSRLQA KVTNTQIFQL QFHTGFIPLD TTVLKFTKPE LDACDVPEKY PQLFQVTLDV
ELQPHDKVME LTPPWEHYCT KDVNPSILFS SHQEHQDTLV LGGQAPIDIP PDNPRHFGQG
GFFSTLCWQD QKSEKSFCEE DHAALVNQES EQSDDELLTL SSPHGNANGD KPHAARKPSK
KQQEPAAPAP PEDVDLLGLE GSAVSKNFSS PAAPPSNSEL LSDLFGGGGA AGPVQSGQSG
VDDVFHPSGP TSTQSTPRRS ATSTSASPTL RVGEGATFDP FGAPSKPSGQ DLLGSFLNTA
SASSDPFLQP TRSPSPTVHA SSTPAVNIQP DVSGAWDWHT KPGGFGMGSK SAATSPTGSS
HGTPTHQNKP QTLDPFADLG TLGGSSFASK PSTPTGLGGG FPPLSSPQKA SPQPMGGGWQ
QGGGYNWQQT QSKPQSSMPH SSPQNRPNYN VSFSSMPGGQ NERGKAAANL EGKQKAADFE
DLLSGQGFNA HKDKKGPRTI AEMRKEEMAK EMDPEKLKIL EWIEGKERNI RALLSTMHTV
LWAGETKWKP VGMADLVTPE QVKKVYRKAV LVVHPDKATG QPYEQYAKMI FMELNDAWSE
FENQGQKPLY
//
