DRP2_HUMAN
ID DRP2_HUMAN Reviewed; 957 AA.
AC Q13474; A6ZKI5; A8K1B0; B1B1F3; B4DIZ0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dystrophin-related protein 2;
DE Short=DRP-2;
GN Name=DRP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=T-cell;
RX PubMed=8640231; DOI=10.1038/ng0696-223;
RA Roberts R.G., Freeman T.C., Kendall E., Vetrie D.L.P., Dixon A.K.,
RA Shaw-Smith C., Bone Q., Bobrow M.;
RT "Characterization of DRP2, a novel human dystrophin homologue.";
RL Nat. Genet. 13:223-226(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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: Required for normal myelination and for normal organization
CC of the cytoplasm and the formation of Cajal bands in myelinating
CC Schwann cells. Required for normal PRX location at appositions between
CC the abaxonal surface of the myelin sheath and the Schwann cell plasma
CC membrane. Possibly involved in membrane-cytoskeleton interactions of
CC the central nervous system. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q05AA6}.
CC -!- SUBUNIT: Interacts with PRX; this enhances phosphorylation. Identified
CC in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD
CC and DAG1. {ECO:0000250|UniProtKB:Q05AA6}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9EPA0}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9EPA0}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9EPA0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q05AA6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q05AA6}. Note=Detected in Schwann cells at
CC periaxonal myelin membranes. {ECO:0000250|UniProtKB:Q05AA6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13474-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13474-2; Sequence=VSP_042662;
CC -!- TISSUE SPECIFICITY: Detected in fetal brain.
CC {ECO:0000269|PubMed:8640231}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI11696.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAF82514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U43519; AAC50538.1; ALT_INIT; mRNA.
DR EMBL; AK289825; BAF82514.1; ALT_INIT; mRNA.
DR EMBL; AK295843; BAG58652.1; -; mRNA.
DR EMBL; AL022155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z68331; CAI42016.2; -; Genomic_DNA.
DR EMBL; Z70281; CAI42016.2; JOINED; Genomic_DNA.
DR EMBL; Z70280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z70281; CAO03505.1; -; Genomic_DNA.
DR EMBL; Z68331; CAO03505.1; JOINED; Genomic_DNA.
DR EMBL; CH471115; EAX02844.1; -; Genomic_DNA.
DR EMBL; BC111695; AAI11696.2; ALT_INIT; mRNA.
DR CCDS; CCDS14480.2; -. [Q13474-1]
DR CCDS; CCDS55465.1; -. [Q13474-2]
DR RefSeq; NP_001164655.1; NM_001171184.1. [Q13474-2]
DR RefSeq; NP_001930.2; NM_001939.2. [Q13474-1]
DR AlphaFoldDB; Q13474; -.
DR SMR; Q13474; -.
DR BioGRID; 108155; 5.
DR IntAct; Q13474; 2.
DR MINT; Q13474; -.
DR STRING; 9606.ENSP00000378635; -.
DR iPTMnet; Q13474; -.
DR PhosphoSitePlus; Q13474; -.
DR BioMuta; DRP2; -.
DR DMDM; 212286371; -.
DR jPOST; Q13474; -.
DR MassIVE; Q13474; -.
DR MaxQB; Q13474; -.
DR PaxDb; Q13474; -.
DR PeptideAtlas; Q13474; -.
DR PRIDE; Q13474; -.
DR ProteomicsDB; 59471; -. [Q13474-1]
DR ProteomicsDB; 59472; -. [Q13474-2]
DR Antibodypedia; 506; 68 antibodies from 17 providers.
DR DNASU; 1821; -.
DR Ensembl; ENST00000395209.8; ENSP00000378635.3; ENSG00000102385.13. [Q13474-1]
DR Ensembl; ENST00000402866.5; ENSP00000385038.1; ENSG00000102385.13. [Q13474-1]
DR Ensembl; ENST00000538510.1; ENSP00000441051.1; ENSG00000102385.13. [Q13474-1]
DR Ensembl; ENST00000541709.5; ENSP00000444752.1; ENSG00000102385.13. [Q13474-2]
DR GeneID; 1821; -.
DR KEGG; hsa:1821; -.
DR MANE-Select; ENST00000395209.8; ENSP00000378635.3; NM_001939.3; NP_001930.2.
DR UCSC; uc004egz.3; human. [Q13474-1]
DR CTD; 1821; -.
DR DisGeNET; 1821; -.
DR GeneCards; DRP2; -.
DR GeneReviews; DRP2; -.
DR HGNC; HGNC:3032; DRP2.
DR HPA; ENSG00000102385; Tissue enhanced (brain, lymphoid tissue).
DR MalaCards; DRP2; -.
DR MIM; 300052; gene.
DR neXtProt; NX_Q13474; -.
DR OpenTargets; ENSG00000102385; -.
DR PharmGKB; PA27486; -.
DR VEuPathDB; HostDB:ENSG00000102385; -.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000153467; -.
DR HOGENOM; CLU_001187_0_0_1; -.
DR InParanoid; Q13474; -.
DR OMA; QADHVMD; -.
DR PhylomeDB; Q13474; -.
DR TreeFam; TF337303; -.
DR PathwayCommons; Q13474; -.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; Q13474; -.
DR BioGRID-ORCS; 1821; 10 hits in 697 CRISPR screens.
DR ChiTaRS; DRP2; human.
DR GenomeRNAi; 1821; -.
DR Pharos; Q13474; Tbio.
DR PRO; PR:Q13474; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13474; protein.
DR Bgee; ENSG00000102385; Expressed in trigeminal ganglion and 118 other tissues.
DR ExpressionAtlas; Q13474; baseline and differential.
DR Genevisible; Q13474; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR CDD; cd00176; SPEC; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR017433; Dystrophin-related_2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF038205; Dystrophin-related_p2; 1.
DR SMART; SM00150; SPEC; 2.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Synapse; Zinc;
KW Zinc-finger.
FT CHAIN 1..957
FT /note="Dystrophin-related protein 2"
FT /id="PRO_0000076083"
FT REPEAT 102..179
FT /note="Spectrin 1"
FT REPEAT 231..337
FT /note="Spectrin 2"
FT DOMAIN 358..383
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 605..661
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 877..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 637
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05AA6"
FT MOD_RES 910
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05AA6"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042662"
FT VARIANT 68
FT /note="V -> L (in dbSNP:rs7066252)"
FT /id="VAR_033898"
FT CONFLICT 73
FT /note="P -> L (in Ref. 2; BAF82514)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="G -> A (in Ref. 1; AAC50538)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="E -> G (in Ref. 2; BAF82514)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> D (in Ref. 1; AAC50538)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="A -> P (in Ref. 1; AAC50538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 957 AA; 107962 MW; 95B26DCFF45DDE12 CRC64;
MQPMVMQGCP YTLPRCHDWQ AADQFHHSSS LRSTCPHPQV RAAVTSPAPP QDGAGVPCLS
LKLLNGSVGA SGPLEPPAMN LCWNEIKKKS HNLRARLEAF SDHSGKLQLP LQEIIDWLSQ
KDEELSAQLP LQGDVALVQQ EKETHAAFME EVKSRGPYIY SVLESAQAFL SQHPFEELEE
PHSESKDTSP KQRIQNLSRF VWKQATVASE LWEKLTARCV DQHRHIERTL EQLLEIQGAM
EELSTTLSQA EGVRATWEPI GDLFIDSLPE HIQAIKLFKE EFSPMKDGVK LVNDLAHQLA
ISDVHLSMEN SQALEQINVR WKQLQASVSE RLKQLQDAHR DFGPGSQHFL SSSVQVPWER
AISPNKVPYY INHQAQTTCW DHPKMTELYQ TLADLNNIKF SAYRTAMKLR RVQKALRLDL
VTLTTALEIF NEHDLQASEH VMDVVEVIHC LTALYERLEE ERGILVNVPL CVDMSLNWLL
NVFDSGRSGK MRALSFKTGI ACLCGTEVKE KLQYLFSQVA NSGSQCDQRH LGVLLHEAIQ
VPRQLGEVAA FGGSNVEPSV RSCFRFSTGK PVIEASQFLE WVNLEPQSMV WLAVLHRVTI
AEQVKHQTKC SICRQCPIKG FRYRSLKQFN VDICQTCFLT GRASKGNKLH YPIMEYYTPT
TSSENMRDFA TTLKNKFRSK HYFSKHPQRG YLPVQSVLEA DYSETPASSP MWPHADTHSR
IEHFASRLAE MESQNCSFFN DSLSPDDSID EDQYLLRHSS PITDREPAFG QQAPCSVATE
SKGELQKILA HLEDENRILQ GELRRLKWQH EEAAEAPSLA DGSTEAATDH RNEELLAEAR
ILRQHKSRLE TRMQILEDHN KQLESQLQRL RELLLQPPTE SDGSGSAGSS LASSPQQSEG
SHPREKGQTT PDTEAADDVG SKSQDVSLCL EDIMEKLRHA FPSVRSSDVT ANTLLAS
