DMD_PIG
ID DMD_PIG Reviewed; 3674 AA.
AC Q5GN48;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dystrophin;
GN Name=DMD {ECO:0000312|EMBL:CAI26302.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAI26302.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Retina {ECO:0000269|PubMed:15941659};
RX PubMed=15941659; DOI=10.1016/j.nmd.2005.03.011;
RA Bordais A., Bolanos-Jimenez F., Fort P., Varela C., Sahel J.A., Picaud S.,
RA Rendon A.;
RT "Molecular cloning and protein expression of Duchenne muscular dystrophy
RT gene products in porcine retina.";
RL Neuromuscul. Disord. 15:476-487(2005).
CC -!- FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-
CC actin. Ligand for dystroglycan. Component of the dystrophin-associated
CC glycoprotein complex which accumulates at the neuromuscular junction
CC (NMJ) and at a variety of synapses in the peripheral and central
CC nervous systems and has a structural function in stabilizing the
CC sarcolemma. Also implicated in signaling events and synaptic
CC transmission. {ECO:0000250|UniProtKB:P11531}.
CC -!- SUBUNIT: Interacts with SYNM (By similarity). Interacts with the
CC syntrophins SNTG1 and SNTG2. Interacts with KRT19. Component of the
CC dystrophin-associated glycoprotein complex which is composed of three
CC subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA
CC and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the
CC transmembrane dystroglycan complex, and the sarcoglycan-sarcospan
CC complex. Interacts with DAG1 (betaDAG1) with DMD; the interaction is
CC inhibited by phosphorylation on the PPXY motif of DAG1 (By similarity).
CC Interacts with SYNM; SNTA1 and SNTB1. Interacts with CMYA5. Directly
CC interacts with ANK2 and ANK3; these interactions do not interfere with
CC betaDAG1-binding and are necessary for proper localization in muscle
CC cells. Identified in a dystroglycan complex that contains at least PRX,
CC DRP2, UTRN, DMD and DAG1 (By similarity). Interacts with DTNB (By
CC similarity). Interacts with PGM5; the interaction is direct (By
CC similarity). {ECO:0000250|UniProtKB:P11530,
CC ECO:0000250|UniProtKB:P11531, ECO:0000250|UniProtKB:P11532}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P11531}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P11531}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P11531}. Note=In muscle cells, sarcolemma
CC localization requires the presence of ANK2, while localization to
CC costameres requires the presence of ANK3. Localizes to neuromuscular
CC junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2
CC presence, but not in newborn animals. {ECO:0000250|UniProtKB:P11531}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:15941659};
CC IsoId=Q5GN48-1; Sequence=Displayed;
CC Name=3 {ECO:0000269|PubMed:15941659}; Synonyms=Dp71
CC {ECO:0000269|PubMed:15941659};
CC IsoId=Q5GN48-3; Sequence=VSP_051967, VSP_051968, VSP_051969;
CC Name=4 {ECO:0000269|PubMed:15941659}; Synonyms=Dp74
CC {ECO:0000269|PubMed:15941659};
CC IsoId=Q5GN48-4; Sequence=VSP_051967, VSP_051968, VSP_051971;
CC Name=5 {ECO:0000269|PubMed:15941659}; Synonyms=Dp71-74
CC {ECO:0000269|PubMed:15941659};
CC IsoId=Q5GN48-5; Sequence=VSP_051967, VSP_051968, VSP_051970;
CC Name=2 {ECO:0000269|PubMed:15941659}; Synonyms=Dp260
CC {ECO:0000269|PubMed:15941659};
CC IsoId=Q5GN48-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: In the retina, expressed in the outer plexiform
CC layer (OPL) and around the blood vessels. Also observed at the vitreal
CC border of the retina corresponding to the inner limiting membrane
CC (ILM). Presynaptically localized in cone pedicles and postsynaptically
CC in bipolar cells (at protein level). {ECO:0000269|PubMed:15941659}.
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DR EMBL; AJ865385; CAI26302.1; -; mRNA.
DR RefSeq; NP_001012408.1; NM_001012408.1. [Q5GN48-1]
DR SMR; Q5GN48; -.
DR STRING; 9823.ENSSSCP00000030238; -.
DR PaxDb; Q5GN48; -.
DR PeptideAtlas; Q5GN48; -.
DR PRIDE; Q5GN48; -.
DR GeneID; 497636; -.
DR KEGG; ssc:497636; -.
DR CTD; 1756; -.
DR eggNOG; KOG4286; Eukaryota.
DR InParanoid; Q5GN48; -.
DR OrthoDB; 72477at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 10.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035436; Dystrophin/utrophin.
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; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 17.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 22.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Metal-binding; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc;
KW Zinc-finger.
FT CHAIN 1..3674
FT /note="Dystrophin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000227522"
FT DOMAIN 11..115
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 130..236
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 335..443
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 444..552
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 555..663
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 715..824
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 826..930
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 939..1041
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 1044..1150
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1153..1259
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1262..1363
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1364..1459
FT /note="Spectrin 10"
FT REPEAT 1464..1564
FT /note="Spectrin 11"
FT REPEAT 1567..1672
FT /note="Spectrin 12"
FT REPEAT 1675..1774
FT /note="Spectrin 13"
FT REPEAT 1775..1870
FT /note="Spectrin 14"
FT REPEAT 1873..1975
FT /note="Spectrin 15"
FT REPEAT 1988..2097
FT /note="Spectrin 16"
FT REPEAT 2100..2204
FT /note="Spectrin 17"
FT REPEAT 2207..2314
FT /note="Spectrin 18"
FT REPEAT 2315..2412
FT /note="Spectrin 19"
FT REPEAT 2464..2566
FT /note="Spectrin 20"
FT REPEAT 2569..2675
FT /note="Spectrin 21"
FT REPEAT 2678..2791
FT /note="Spectrin 22"
FT REPEAT 2797..2919
FT /note="Spectrin 23"
FT REPEAT 2924..3029
FT /note="Spectrin 24"
FT DOMAIN 3044..3077
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3297..3353
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..236
FT /note="Actin-binding"
FT REGION 59..68
FT /note="ANK2- and ANK-3 binding"
FT /evidence="ECO:0000250"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1909
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250"
FT REGION 3047..3397
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250"
FT REGION 3455..3507
FT /note="Binds to SNTB1"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT REGION 3517..3543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3590..3674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3591..3662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 3472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT VAR_SEQ 1
FT /note="M -> MREQLKG (in isoform 3, isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15941659"
FT /id="VSP_051967"
FT VAR_SEQ 2..3064
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15941659"
FT /id="VSP_051968"
FT VAR_SEQ 3397..3410
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15941659"
FT /id="VSP_051969"
FT VAR_SEQ 3398..3507
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15941659"
FT /id="VSP_051970"
FT VAR_SEQ 3454..3507
FT /note="IDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEE
FT NR -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15941659"
FT /id="VSP_051971"
SQ SEQUENCE 3674 AA; 424858 MW; 03C22FB8D805632C CRC64;
MSEVSSDERE DVQKKTFTKW INAQFSKFGK QHIENLFNDL QDGRRLLDLL EGLTGQKLPK
EKGSTRVHAL NNVNKALQVL QKNNVDLVNI GSTDIVDGNH KLTLGLIWNI ILHWQVKNVM
KNIMAGLQQT NSEKILLSWV RQSTRNYPQV NVINFTTSWS DGLALNALIH SHRPDLFDWN
SVVCQQSATQ RLEHAFNIAK YQLGIEKLLD PEDVATTYPD KKSILMYVTS LFQVLPQQVS
IEAIQEVEML PRPSKVTREE HFQLHHQMHY SQQITVCLAQ GYERTPSPKP RFKSYAYTQA
AYVTTSDPTR SPFPSQRLES PEDKSFGSSL LETEVNLDSY QTALEEVLSW LLSAEDTLQA
QGEISNDVEE VKEQFHTHEG YMMDLTSHQG RIGSVLQLGS QLIGKGKLSE DEETEVQEQM
NLLNSRWECL RVASVEKQSN LHKVLMDLQN QQLKELNDWL TKTEEKTRKM EKEPLGPDLE
DLKHQIQQHK VLQEDLEQEQ VRVNSLTHMV VVVDESSGDH ATAALEEQLK VLGDRWANIC
RWTEDRWVLL QDILLKWQRF TEEQCLFSTW LSEKEDALNK IHTTGFKDQG EMLSSLQKLA
VLKTDLEKKK QTMDKLSSLN QDLLSTLKNT LVAQKMEAWL DNFAQRWDNL VQKLEKSSTQ
ISQAVTTTQP SLTQTTVMET VTMVTTREQI LVKHAQEELP PPPPQKKRQI IVDSEIRKRL
DVDITELHSW ITRSEAVLQS PEFAIYRKEG NFSDLKEKVN AIEREKAEKF RKLQDASRSA
QALVEQMVNE GVNADSIKQA AEQLNSRWIE FCQLLSERLN WLEYQNRIIT FYNQLQQLEQ
ITTAAENWLK TQPITTSEPT AVKSQLKICK DEVNRLSALQ PQIERLKIES IALKEKGQGP
MFLDADSVAF TNHFNQVFAD MQAKEKELQI IFDTLPPMRY QETMSTILTW IQHSEAKLSI
PQATVTEYEI MEQRLGELQA LQSSLQEQQN GLNYLSTTVK EMSKKAPSNI SRKYQSEFEE
IEGRWKKLSA QLMEHCQKLE EQIAKLRKLQ NHIKTLKNWM AEVDIFLKEE WPALGDSEIL
RKQLKQCRLL VSDIQTIQPS LNSVNEGGQK IKKEAEPEFA SRLETELREL NTQWDYICRQ
VYARKEALKG GLDKTISLQK DLSEMHEWMT QAEEEYLERD FEYKTPDELQ TAVEEMKRAK
EEAQQKEAKV KLLTESVNSV IAQAPPAAQE ALKKELDTLT TNYQWLCTRL NGKCKTLEEV
WACWHELLSY LEKANKWLSE VEFKLKTTEN IPGGAEEISE VLESLENLMQ HSEDNPNQIR
ILAQTLTDGG VMDELINEEL ETFNSRWREL HEEAVRRQKL LEQSIQSAQE IEKSLHLIQD
SLSSIDHQLA VYIADKVDAA QMPQEAQKIQ SDLTSHEISL EEMKKHYQGK EAAPRVLSQI
ELAQKKLQDV SMKFRLFQKP ANFEQRLQES KMILDEVKMH LPALEIKSVE QEVVQSQLNH
CVNLYKSLSE VKSEVEMVIK TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ
QLEKCLKLSR KMRKEMNVLT EWLAATDTEL TKRSAVEGMP SNLDSEVVWG KATQKEIEKQ
KFHLKSISEI GEALKMVLGK KETLVEDKLS LLNSNWIAVT SRAEEWLNLL LEYQKHMENF
DQNVDHITKW IIQADTLLDE SEKKKPQQKE DVLKRLKAEM NDMRPKVDST RDQAANLMAN
RGDHCRKVIE PKISELNHRF AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG
VNLKEEDFNK DMSEDNEGTV KELLQRGDNL QQRITDERKR EEIKIKQQLL QTKHNALKDL
RSQRRKKALE ISHQWYQYKR QADDLLKCLD DIEKKLASLP EPQDEKKIKE IDRELQKKKE
ELDAVRRQAE GLSEDGAAMA VEPTQIQLSK RWREIESKFA HFRRLNFAQI HTVHEESVMV
MTEDMPLEIS YVPSAYLTEI THVSQALSEV EQLLNAPDLC AKDFEDLFKQ EESLKNIKDS
LQQISGRVDI IHNKKTAGLQ SATPVERTRL QEALSQLDFQ WERVNKMYKD RQGKFDRSVE
KWRRFHYDMK IFNQWLTEAE HFLKKTQIPE NWEHAKYKWY LKELQDGIGQ RQTIVRVLNA
TGEEVIQQSS KTDASILQEK LGSLNLRWQE VCKQLAERKK RLEEQKNILS EFQRDLNEFV
LWLEEADNIT SVALEPGNEQ QLKEKLEEIK LLAEELPLRQ GTLKQLNETG GTVLVSAPIS
PEEQDKIENK LKQTNLQWIK VSRILPEKQG EIEAHIKDLG QFEEQLNHLL VWLSPIKNQL
EIYNQPNQTG PFDIKETEVA VQAKQLDVEG ILSKGQHLYK EKPATQPVKR KLEDLSSEWK
AVTHLLQELR AKWPGPTPGL TTIEAPTSQT VTLVTQPTVT KETAISKPEM PSSLLLEVPA
LADFNRAWTE LTDWLSLLDR VIKSQRVMVG DLEDINEMII KQKATLQDLE QRRPQLEELI
TAAQNLKNKT SNQEARTIIT DRIERIQSQW DEVQEHLQNR RQQLNEMLKD STQWLEAKEE
AEQVLGQARA KLESWKEGPY TMDAIQRKIT ETKQLAKDLR QWQINVDVAN DLALKLLRDY
SADDTRKVHM ITENINASWA NIHKRLSERE TVLEETHRLL QQFPLDLEKF LAWLTEAETT
ANVLQDATHK ERLLEDSKGV RELMKQWQDL QGEIEAHTDI YHNLDENGQK ILRSLEGSDD
AILLQRRLDN MNFKWSELRK KSLNIRSHLE ASSDQWKRLH LSLQELLVWL QLKDDELSRQ
APIGGDCPAV QKQNDVHRAF KRELKTKEPV IMSTLETVRI FLTEQPLEGL EKLYQEPREL
PPEERAQNVT RLLRKQAEEV NTEWEKLNLH SADWQRKIDE ALERLQELQE ATDELDLKLR
QAEVIKGSWQ PVGDLLIDSL QDHLEKVKAL RGEKAPLKEN VSHVNDLARQ LTTLGIQLSP
YNLSTLEDLN TRWKLLQVAV EDRIRQLHEA HRDFGPASQH FLSTSVQGPW ERAISPNKVP
YYINHETQTT CWDHPKMTEL YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSLSAACD
ALDQHNLKQN DQPMDILQII NCLTTVYDRL EQEHNNLVNV PLCVDMCLNW LLNVYDTGRT
GRIRVLSFKT GIVSLCKAHL EDKYRYLFKQ VASSTGFCDQ RRLGLLLHDS IQIPRQLGEV
ASFGGSNIEP SVRSCFQFAN NKPEIEAALF LDWMRLEPQS MVWLPVLHRV AAAETAKHQA
KCNICKECPI IGFRYRSLKH FNYDICQSCF FSGRVAKGHK MHYPMVEYCT PTTSGEDVRD
FAKVLKNKFR TKRYFAKHPR MGYLPVQTVL EGDNMETPVT LINFWPVDSA PASSPQLSHD
DTHSRIEHYA SRLAEMENSN GSYLNDSISP NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP
AQILISLESE ERGELERILA DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ
SPRDAELIAE AKLLRQHKGR LEARMQTLED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV
SSPSTSLQRS DSSQPMLLRV VGSQTSESMG EEDLLSPPQD TSTGLEEVME QLNNSFPSSR
GRNTPGKPVR EDTM
