ID PTPRZ_MOUSE Reviewed; 2312 AA.
AC B9EKR1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase zeta;
DE Short=R-PTP-zeta;
DE EC=3.1.3.48 {ECO:0000269|PubMed:16513268};
DE Flags: Precursor;
GN Name=Ptprz1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=9655611; DOI=10.1016/s0304-3940(98)00295-x;
RA Shintani T., Watanabe E., Maeda N., Noda M.;
RT "Neurons as well as astrocytes express proteoglycan-type protein tyrosine
RT phosphatase zeta/RPTPbeta: analysis of mice in which the PTPzeta/RPTPbeta
RT gene was replaced with the LacZ gene.";
RL Neurosci. Lett. 247:135-138(1998).
RN [4]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11003666; DOI=10.1128/mcb.20.20.7706-7715.2000;
RA Harroch S., Palmeri M., Rosenbluth J., Custer A., Okigaki M., Shrager P.,
RA Blum M., Buxbaum J.D., Schlessinger J.;
RT "No obvious abnormality in mice deficient in receptor protein tyrosine
RT phosphatase beta.";
RL Mol. Cell. Biol. 20:7706-7715(2000).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12355066; DOI=10.1038/ng1004;
RA Harroch S., Furtado G.C., Brueck W., Rosenbluth J., Lafaille J., Chao M.,
RA Buxbaum J.D., Schlessinger J.;
RT "A critical role for the protein tyrosine phosphatase receptor type Z in
RT functional recovery from demyelinating lesions.";
RL Nat. Genet. 32:411-414(2002).
RN [6]
RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=16513268; DOI=10.1016/j.neulet.2006.01.045;
RA Tamura H., Fukada M., Fujikawa A., Noda M.;
RT "Protein tyrosine phosphatase receptor type Z is involved in hippocampus-
RT dependent memory formation through dephosphorylation at Y1105 on p190
RT RhoGAP.";
RL Neurosci. Lett. 399:33-38(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572; SER-576; THR-1681 AND
RP THR-1684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
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).
RN [8]
RP INTERACTION WITH CNTN1.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
RN [9]
RP DISRUPTION PHENOTYPE, INTERACTION WITH CNTN1, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=21969550; DOI=10.1073/pnas.1108774108;
RA Lamprianou S., Chatzopoulou E., Thomas J.L., Bouyain S., Harroch S.;
RT "A complex between contactin-1 and the protein tyrosine phosphatase PTPRZ
RT controls the development of oligodendrocyte precursor cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17498-17503(2011).
CC -!- FUNCTION: Protein tyrosine phosphatase that negatively regulates
CC oligodendrocyte precursor proliferation in the embryonic spinal cord.
CC Required for normal differentiation of the precursor cells into mature,
CC fully myelinating oligodendrocytes. May play a role in protecting
CC oligondendrocytes against apoptosis. May play a role in the
CC establishment of contextual memory, probably via the dephosphorylation
CC of proteins that are part of important signaling cascades.
CC {ECO:0000269|PubMed:12355066, ECO:0000269|PubMed:16513268,
CC ECO:0000269|PubMed:21969550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:16513268};
CC -!- SUBUNIT: The carbonic-anhydrase like domain interacts with CNTN1
CC (contactin) (PubMed:20133774, PubMed:21969550). Interaction with PTN
CC promotes formation of homooligomers; oligomerization impairs
CC phosphatase activity (By similarity). Interacts (via chondroitin
CC sulfate chains) with MDK (via C-terminal); this interaction is
CC inhibited by PTN; this interaction promotes neuronal migration (By
CC similarity). {ECO:0000250|UniProtKB:Q62656,
CC ECO:0000269|PubMed:20133774, ECO:0000269|PubMed:21969550}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21969550};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:21969550}.
CC Secreted {ECO:0000269|PubMed:21969550}. Note=A secreted form is
CC apparently generated by shedding of the extracellular domain.
CC -!- TISSUE SPECIFICITY: Detected in neurons and astrocytes in the central
CC nervous system (CNS). Detected in the hippocampus and in brain cortex.
CC {ECO:0000269|PubMed:11003666, ECO:0000269|PubMed:9655611}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC expected Mendelian rate, are viable and fertile (PubMed:11003666).
CC Embryonic mutant mice show increased levels of oligodendrocyte
CC precursor cells in the spinal cord, combined with impaired
CC differentiation of the precursor cells into mature, fully myelinating
CC oligodendrocytes (PubMed:21969550). Mutant mice show slightly increased
CC susceptibility to experimental autoimmune encephalomyelitis (EAE) and
CC strongly reduced recovery. Contrary to wild-type, mutant mice remain
CC paralyzed and display increased levels of apoptotic oligodendrocytes in
CC the spinal cord (PubMed:12355066). Besides, mutant mice display
CC impaired contextual fear memory, probably due to impaired
CC dephosphorylation of proteins that are part of important signaling
CC cascades (PubMed:16513268). {ECO:0000269|PubMed:11003666,
CC ECO:0000269|PubMed:12355066, ECO:0000269|PubMed:16513268,
CC ECO:0000269|PubMed:21969550}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily. {ECO:0000305}.
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DR EMBL; AC133599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151071; AAI51072.1; -; mRNA.
DR CCDS; CCDS39437.1; -.
DR RefSeq; NP_001074775.1; NM_001081306.1.
DR AlphaFoldDB; B9EKR1; -.
DR SMR; B9EKR1; -.
DR BioGRID; 202509; 6.
DR IntAct; B9EKR1; 4.
DR MINT; B9EKR1; -.
DR STRING; 10090.ENSMUSP00000088056; -.
DR GlyConnect; 2675; 10 N-Linked glycans (3 sites).
DR GlyCosmos; B9EKR1; 10 sites, 10 glycans.
DR GlyGen; B9EKR1; 11 sites, 10 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; B9EKR1; -.
DR PhosphoSitePlus; B9EKR1; -.
DR SwissPalm; B9EKR1; -.
DR jPOST; B9EKR1; -.
DR MaxQB; B9EKR1; -.
DR PaxDb; 10090-ENSMUSP00000088056; -.
DR PeptideAtlas; B9EKR1; -.
DR ProteomicsDB; 291796; -.
DR Pumba; B9EKR1; -.
DR Antibodypedia; 2175; 232 antibodies from 26 providers.
DR DNASU; 19283; -.
DR Ensembl; ENSMUST00000090568.7; ENSMUSP00000088056.4; ENSMUSG00000068748.8.
DR GeneID; 19283; -.
DR KEGG; mmu:19283; -.
DR UCSC; uc009bba.1; mouse.
DR AGR; MGI:97816; -.
DR CTD; 5803; -.
DR MGI; MGI:97816; Ptprz1.
DR VEuPathDB; HostDB:ENSMUSG00000068748; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000155529; -.
DR HOGENOM; CLU_001120_1_0_1; -.
DR InParanoid; B9EKR1; -.
DR OMA; DPINCES; -.
DR OrthoDB; 2903434at2759; -.
DR PhylomeDB; B9EKR1; -.
DR TreeFam; TF351978; -.
DR Reactome; R-MMU-201556; Signaling by ALK.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR BioGRID-ORCS; 19283; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Ptprz1; mouse.
DR PRO; PR:B9EKR1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; B9EKR1; Protein.
DR Bgee; ENSMUSG00000068748; Expressed in vestibular membrane of cochlear duct and 203 other cell types or tissues.
DR ExpressionAtlas; B9EKR1; baseline and differential.
DR Genevisible; B9EKR1; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0072534; C:perineuronal net; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; ISO:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IMP:UniProtKB.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd17669; R-PTP-Z-2; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF461; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ZETA; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..2312
FT /note="Receptor-type tyrosine-protein phosphatase zeta"
FT /id="PRO_0000424882"
FT TOPO_DOM 25..1637
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1638..1658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1659..2312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..300
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT DOMAIN 314..413
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1714..1989
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 2020..2279
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 428..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1930
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1898
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1930..1936
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1974
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 2220
FT /note="Ancestral active site"
FT /evidence="ECO:0000250"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62656"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62656"
FT MOD_RES 1681
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1684
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2052
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23471"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1058
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..240
FT /evidence="ECO:0000250"
FT DISULFID 133..264
FT /evidence="ECO:0000250"
SQ SEQUENCE 2312 AA; 254405 MW; 91C5D58F74BA999C CRC64;
MRILQSFLAC VQLLCLCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK
QSPINIDEDL TQVNVNLKKL KFQGWEKASL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV
FKASKITFHW GKCNVSSEGS EHSLEGQKFP LEMQVYCFDA DRFSSFEEAV KGKGRLRALS
ILFEVGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFVLQNL LPNSTDKYYI YNGSLTSPPC
TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
TGKEEIHEVV CSSEPENVQA DPENYTSLLV TWERPRVVYD AMIEKFAVLY QPLAGNDQAK
HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCSNGLYGKY SDQLIVDMPT EDAELDLFPE
LIGTEEIIKE EEYGKDNEED TGLNPGRDSV TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN
RSPTRGSEFS GKSDVPNTSP NSTSQHVAEF ETERGISLPS QTGTNLPPHN VEGTSASLNS
GSKTLFIFPQ MNLSGTAESL NTVPITEYKE VSADVSEEEN FLTDFKLDTG ADDSSGSSPS
TSTVPFSSDN LSHGYITSSD MPEAITYDVL KPGSTRNAPE DSAPSGSEES LKDPSLEGSV
WFPGSTDLTT QSETGSGRES FLQVNSTDIQ IDESRETTES FSPDATVSQD PSVTDMGMPH
YSTFAYLPTE VTPQAFTPSS RPLDLAPTIN ILHSQTTQPV YNGETPLQPS YSSEVFPLAT
PLLLDNQTLN TTPAASSSDS ALHATPVSPS VGVSFESILS SYDDAPLLPF SSASFSSEMF
RHLHTVSQTL PQVTSAAERD ELSLHASLLV ARGDLLLEPS LVQYSDVASH QATTRAASDT
LGFGSESAVF YKTSMVSQIE SPRSDVVMHA YSSGPEPSYT VEGSHHVPTV SYSSAMPLHG
SVDVSDQGSL LINPSHISMP ESSFITPTAS LLQPPPALSG DGEWSGASSD SELLLPDADG
LRTLNISSPV SVAEFTYTTS VFADGIKPLS KSEMMYGNET ELKMSSFSDM AYPSKSTVVP
KMSDVVHKWS ESLKETSVSI SSMKSVFPES LVYPTTKGFE QGVSHVPEII FPVQPTHTAS
QASGDTWLKP GLSANSEAAF SDTASREVVH PSTQPLLYEA ATPFNTEALL QPSFQASDVD
TLLKTALPSV PSDPILAGTP QVEQSSSSVS HPMASESGSS ESMLHFTSVP ILDISPSKVH
STPLQGLTVP HSSKKFSEQG LLKSKSPQQV LPSLFSNDEF FQSAHLDVSQ AYPPKGRHAF
VTPVLSIDEP QNTLINKLVY SEDIFSSTEI SITDKVLTGL PTLASDVLSS TDHSVPLGSG
PISLTMVSPN RDDSVTTAKL LLPSTATSKL TQSARSDADL VGGGEDGDDY DDDDYDDIDR
GRFPVNKCMS CLPYRESREK VMNDSDTQES SLVDQSDPIS PLLFENTEEE NGGTGVTRVD
KSPPPSMLPQ NHNDGKEDSD IQMGSAVLPH TPGSKAWAVL TSDEESGSGQ GTSDSLNDNE
TSTDFSFPDV NEKDTDGVLE TDDTGIAPGS PRSSTPSVTS GHSGVSNSSE AEASNSSHES
RIGLAEGLES EKKAVIPLVI VSALTFICLV VLVGILIYWR KCFQTAHFYL EDNTSPRVIS
TPPTPIFPIS DDIGAIPIKH FPKHVADLHA SNGFTEEFET LKEFYQEVQS CTADLGITAD
SSNHPDNKHK NRYVNIVAYD HSRVKLTQLA EKDGKLTDYI NANYVDGYNR PKAYIAAQGP
LKSTAEDFWR MIWEHNVEVI VMITNLVEKG RRKCDQYWPT DGSEEYGSFL VNQKSVQVLA
YYTVRNFTLR NTKLKKGSQK GRSSGRLVTQ YHYTQWPDMG VPEYSLPVLA FVRKAAQAKR
HAVGPVVVHC SAGVGRTGTY IVLDSMLQQI QHEGTVNIFG FLKHIRSQRN YLVQTEEQYV
FIHDTLVEAI LSKETEVPDS HIHSYVNTLL IPGPTGKTKL EKQFQLLSQS NILQSDYSTA
LKQCNREKNR TSSIIPVERS RVGISSLSGE GTDYINASYI MGYYQSNEFI ITQHPLLHTI
KDFWRMIWDH NAQLVVMIPD GQNMAEDEFV YWPNKDEPIN CESFKVTLMS EEHKCLSNEE
KLIVQDFILE ATQDDYVLEV RHFQCPKWPN PDSPISKTFE LISIIKEEAA NRDGPMIVHD
EHGGVTAGTF CALTTLMHQL EKENAMDVYQ VAKMINLMRP GVFTDIEQYQ FLYKVVLSLV
STRQEENPST SLDSNGAALP DGNIAESLES LV
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