SMAD2_RAT
ID SMAD2_RAT Reviewed; 467 AA.
AC O70436; A0JPM1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Mothers against decapentaplegic homolog 2;
DE Short=MAD homolog 2;
DE Short=Mothers against DPP homolog 2;
DE AltName: Full=Mad-related protein 2;
DE AltName: Full=SMAD family member 2;
DE Short=SMAD 2;
DE Short=Smad2;
GN Name=Smad2; Synonyms=Madh2;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10382592; DOI=10.1007/s001250051220;
RA Zhang Y.-Q., Kanzaki M., Furukawa M., Shibata H., Ozeki M., Kojima I.;
RT "Involvement of Smad proteins in the differentiation of pancreatic AR42J
RT cells induced by activin A.";
RL Diabetologia 42:719-727(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10670756; DOI=10.1507/endocrj.46.695;
RA Osaki M., Tsukazaki T., Ono N., Yonekura A., Hirota Y., Miyazaki Y.,
RA Shindo H., Sonta S., Yamashita S.;
RT "cDNA cloning and chromosomal mapping of rat Smad2 and Smad4 and their
RT expression in cultured rat articular chondrocytes.";
RL Endocr. J. 46:695-701(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
RA Kato S., Sano A., Suto T., Nakagawa K., Nakahara Y., Haraguchi N.,
RA Higashi K.;
RT "Molecular cloning of rat Smad2 gene.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
CC -!- FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular
CC signal transducer and transcriptional modulator activated by TGF-beta
CC (transforming growth factor) and activin type 1 receptor kinases. Binds
CC the TRE element in the promoter region of many genes that are regulated
CC by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates
CC transcription. May act as a tumor suppressor in colorectal carcinoma.
CC Positively regulates PDPK1 kinase activity by stimulating its
CC dissociation from the 14-3-3 protein YWHAQ which acts as a negative
CC regulator (By similarity). {ECO:0000250|UniProtKB:Q15796,
CC ECO:0000250|UniProtKB:Q62432}.
CC -!- SUBUNIT: Monomer; in the absence of TGF-beta (By similarity).
CC Heterodimer; in the presence of TGF-beta (By similarity). Forms a
CC heterodimer with co-SMAD, SMAD4, in the nucleus to form the
CC transactivation complex SMAD2/SMAD4 (By similarity). Found in a complex
CC with SMAD3 and TRIM33 upon addition of TGF-beta (By similarity).
CC Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
CC SMAD4 (By similarity). Interacts (via the MH2 domain) with ZFYVE9; may
CC form trimers with the SMAD4 co-SMAD (By similarity). Interacts with
CC TAZ/WWRT1 (By similarity). Interacts with FOXH1 (By similarity).
CC Interacts with SNW1 (By similarity). Interacts with CREB-binding
CC protein (CBP) and EP300 (By similarity). Interacts with SNON (By
CC similarity). Interacts with ALK4/ACVR1B (By similarity). Interacts with
CC SKOR1 (By similarity). Interacts with SKOR2 (By similarity). Interacts
CC with PRDM16 (By similarity). Interacts (via MH2 domain) with LEMD3 (By
CC similarity). Interacts with RBPMS (By similarity). Interacts with WWP1.
CC Interacts (dephosphorylated form, via the MH1 and MH2 domains) with
CC RANBP3 (via its C-terminal R domain); the interaction results in the
CC export of dephosphorylated SMAD3 out of the nucleus and termination of
CC the TGF-beta signaling (By similarity). Interacts with PDPK1 (via PH
CC domain) (By similarity). Interacts with DAB2; the interactions are
CC enhanced upon TGF-beta stimulation (By similarity). Interacts with
CC USP15 (By similarity). Interacts with PPP5C (By similarity). Interacts
CC with LDLRAD4 (via the SMAD interaction motif) (By similarity).
CC Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif)
CC (By similarity). Interacts with ZFHX3 (By similarity). Interacts with
CC ZNF451 (By similarity). Interacts with SMURF2 when phosphorylated on
CC Ser-465/467 (By similarity). Interacts with PPM1A (By similarity).
CC Interacts with TGF-beta (By similarity). Interacts with TGFBR1 (By
CC similarity). Interacts with TGIF (By similarity). Interacts with SMAD3
CC and TRIM33 (By similarity). Interacts with ZNF580 (By similarity).
CC Interacts with NEDD4L in response to TGF-beta (By similarity).
CC Interacts with HGS (By similarity). Interacts with AIP1 (By
CC similarity). Interacts with WWP1 (By similarity). Interacts with PML
CC (By similarity). Interacts weakly with ZNF8 (By similarity). Interacts
CC (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the
CC transcriptional responses by mediating ubiquitination and degradation
CC of SMAD2 inhibitors (By similarity). Interacts with YAP1 (when
CC phosphorylated at 'Ser-112') (By similarity).
CC {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
CC -!- INTERACTION:
CC O70436; P47196: Akt1; NbExp=2; IntAct=EBI-7948047, EBI-7204362;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus
CC {ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the
CC absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates
CC to the nucleus when complexed with SMAD4 (By similarity). On
CC dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4
CC complex, and exported out of the nucleus by interaction with RANBP1 (By
CC similarity). Localized mainly to the nucleus in the early stages of
CC embryo development with expression becoming evident in the cytoplasm at
CC the blastocyst and epiblast stages (By similarity).
CC {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
CC -!- PTM: In response to TGF-beta, phosphorylated on the C-terminal SXS
CC motif by TGF-beta and activin type 1 receptor kinases, phosphorylation
CC declines progressively in a KMT5A-dependent manner. Phosphorylation in
CC this motif is required for interaction with a number of proteins
CC including SMURF2, SNON and SMAD4 in response to TGF-beta.
CC Dephosphorylated in this motif by PPM1A leading to disruption of the
CC SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta
CC signaling. In response to decorin, the naturally occurring inhibitor of
CC TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated
CC by MAPK3 upon EGF stimulation; which increases transcriptional activity
CC and stability, and is blocked by calmodulin. Phosphorylated by PDPK1
CC (By similarity). {ECO:0000250|UniProtKB:Q15796}.
CC -!- PTM: Acetylated on Lys-19 by coactivators in response to TGF-beta
CC signaling, which increases transcriptional activity.
CC {ECO:0000250|UniProtKB:Q15796}.
CC -!- PTM: In response to TGF-beta, ubiquitinated by NEDD4L; which promotes
CC its degradation. Monoubiquitinated, leading to prevent DNA-binding (By
CC similarity). Deubiquitination by USP15 alleviates inhibition and
CC promotes activation of TGF-beta target genes (By similarity).
CC Ubiquitinated by RNF111, leading to its degradation: only SMAD2
CC proteins that are 'in use' are targeted by RNF111, RNF111 playing a key
CC role in activating SMAD2 and regulating its turnover (By similarity).
CC {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; AB017912; BAA33453.1; -; mRNA.
DR EMBL; AF056001; AAC12780.1; -; mRNA.
DR EMBL; AB010147; BAA81909.1; -; mRNA.
DR EMBL; BC127497; AAI27498.1; -; mRNA.
DR RefSeq; NP_001264379.1; NM_001277450.1.
DR RefSeq; NP_062064.1; NM_019191.2.
DR AlphaFoldDB; O70436; -.
DR SMR; O70436; -.
DR BioGRID; 248011; 2.
DR IntAct; O70436; 1.
DR MINT; O70436; -.
DR STRING; 10116.ENSRNOP00000048329; -.
DR ChEMBL; CHEMBL3784912; -.
DR iPTMnet; O70436; -.
DR PhosphoSitePlus; O70436; -.
DR jPOST; O70436; -.
DR PaxDb; O70436; -.
DR PRIDE; O70436; -.
DR ABCD; O70436; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000092173; ENSRNOP00000075341; ENSRNOG00000018140.
DR GeneID; 29357; -.
DR KEGG; rno:29357; -.
DR CTD; 4087; -.
DR RGD; 3031; Smad2.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000153499; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; O70436; -.
DR OMA; TNMCTIR; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; O70436; -.
DR TreeFam; TF314923; -.
DR Reactome; R-RNO-1181150; Signaling by NODAL.
DR Reactome; R-RNO-1502540; Signaling by Activin.
DR Reactome; R-RNO-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-9617828; FOXO-mediated transcription of cell cycle genes.
DR PRO; PR:O70436; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018140; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; O70436; baseline and differential.
DR Genevisible; O70436; RN.
DR GO; GO:0032444; C:activin responsive factor complex; ISO:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; ISO:RGD.
DR GO; GO:0071142; C:homomeric SMAD protein complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0071141; C:SMAD protein complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0070410; F:co-SMAD binding; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0070411; F:I-SMAD binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; ISO:RGD.
DR GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:RGD.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0030325; P:adrenal gland development; IDA:RGD.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; ISS:UniProtKB.
DR GO; GO:0007182; P:common-partner SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
DR GO; GO:0009880; P:embryonic pattern specification; ISO:RGD.
DR GO; GO:0007492; P:endoderm development; ISO:RGD.
DR GO; GO:0001706; P:endoderm formation; ISO:RGD.
DR GO; GO:0007369; P:gastrulation; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0038092; P:nodal signaling pathway; ISO:RGD.
DR GO; GO:0035265; P:organ growth; ISO:RGD.
DR GO; GO:0031016; P:pancreas development; ISO:RGD.
DR GO; GO:0048340; P:paraxial mesoderm morphogenesis; ISS:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0060039; P:pericardium development; ISO:RGD.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1900224; P:positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0070723; P:response to cholesterol; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
DR GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0007183; P:SMAD protein complex assembly; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; ISO:RGD.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT CHAIN 2..467
FT /note="Mothers against decapentaplegic homolog 2"
FT /id="PRO_0000090854"
FT DOMAIN 10..176
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 274..467
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 207..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..225
FT /note="PY-motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 229..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 240
FT /note="Phosphoserine; by CAMK2"
FT /evidence="ECO:0000250|UniProtKB:Q15796,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15796,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 465
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000250|UniProtKB:Q15796,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 467
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000250|UniProtKB:Q15796,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
SQ SEQUENCE 467 AA; 52239 MW; 3A775444411F6619 CRC64;
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE
LEKAITTQNC NTKCVTIPST CSEIWGLSTA NTVDQWDTTG LYSFSEQTRS LDGRLQVSHR
KGLPHVIYCR LWRWPDLHSH HELKAIENCE YAFSLKKDEV CVNPYHYQRV ETPVLPPVLV
PRHTEILTEL PPLDDYTHSI PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS
MDTGSPAELS PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL SDSAIFVQSP
NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ GFEAVYQLTR MCTIRMSFVK
GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD KVLTQMGSPS VRCSSMS
