PLEC_CRIGR
ID PLEC_CRIGR Reviewed; 4473 AA.
AC Q9JI55;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Plectin;
DE Short=PCN;
DE Short=PLTN;
DE AltName: Full=300 kDa intermediate filament-associated protein;
DE AltName: Full=IFAP300;
DE AltName: Full=Plectin-1;
DE Flags: Fragment;
GN Name=PLEC; Synonyms=PLEC1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10873583; DOI=10.1006/bbrc.2000.2916;
RA Clubb B.H., Chou Y.-H., Herrmann H., Svitkina T.M., Borisy G.G.,
RA Goldman R.D.;
RT "The 300-kDa intermediate filament-associated protein (IFAP300) is a
RT hamster plectin ortholog.";
RL Biochem. Biophys. Res. Commun. 273:183-187(2000).
RN [2]
RP PHOSPHORYLATION AT THR-4328.
RX PubMed=8626512; DOI=10.1074/jbc.271.14.8203;
RA Malecz N., Foisner R., Stadler C., Wiche G.;
RT "Identification of plectin as a substrate of p34cdc2 kinase and mapping of
RT a single phosphorylation site.";
RL J. Biol. Chem. 271:8203-8208(1996).
CC -!- FUNCTION: Interlinks intermediate filaments with microtubules and
CC microfilaments and anchors intermediate filaments to desmosomes or
CC hemidesmosomes. May be involved not only in the cross-linking and
CC stabilization of cytoskeletal intermediate filaments network, but also
CC in the regulation of their dynamics.
CC -!- SUBUNIT: Homodimer or homotetramer (By similarity). Interacts (via
CC actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH)
CC 1 domain) with VIM (via rod region). Interacts (via N-terminus) with
CC DST isoform 2 (via N-terminus). Interacts with FER. Interacts with
CC TOR1A (By similarity). Interacts with ANK3 (By similarity). Identified
CC in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC,
CC PRX and spectrin (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P30427, ECO:0000250|UniProtKB:Q9QXS1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q15149}. Cell junction, hemidesmosome
CC {ECO:0000250|UniProtKB:Q15149}.
CC -!- DOMAIN: The N-terminus interacts with actin, the C-terminus with
CC vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and
CC the C-terminus can bind integrin beta-4.
CC -!- PTM: Phosphorylated by CDK1; regulates dissociation from intermediate
CC filaments during mitosis. {ECO:0000269|PubMed:8626512}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
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DR EMBL; AF260753; AAF70372.1; -; mRNA.
DR SMR; Q9JI55; -.
DR iPTMnet; Q9JI55; -.
DR PRIDE; Q9JI55; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.90.1290.10; -; 6.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR030269; Plectin.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR23169; PTHR23169; 3.
DR PANTHER; PTHR23169:SF20; PTHR23169:SF20; 3.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00681; Plectin; 18.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00250; PLEC; 34.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF75399; SSF75399; 7.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Methylation; Phosphoprotein; Repeat; SH3 domain.
FT CHAIN <1..4473
FT /note="Plectin"
FT /id="PRO_0000078134"
FT DOMAIN <1..74
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 87..192
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 449..508
FT /note="Spectrin 1"
FT REPEAT 529..613
FT /note="Spectrin 2"
FT REPEAT 626..719
FT /note="Spectrin 3"
FT DOMAIN 730..787
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1104..1204
FT /note="Spectrin 4"
FT REPEAT 2615..2652
FT /note="Plectin 1"
FT REPEAT 2653..2690
FT /note="Plectin 2"
FT REPEAT 2691..2728
FT /note="Plectin 3"
FT REPEAT 2729..2766
FT /note="Plectin 4"
FT REPEAT 2770..2804
FT /note="Plectin 5"
FT REPEAT 2905..2942
FT /note="Plectin 6"
FT REPEAT 2943..2980
FT /note="Plectin 7"
FT REPEAT 2981..3018
FT /note="Plectin 8"
FT REPEAT 3019..3056
FT /note="Plectin 9"
FT REPEAT 3057..3094
FT /note="Plectin 10"
FT REPEAT 3274..3311
FT /note="Plectin 11"
FT REPEAT 3312..3349
FT /note="Plectin 12"
FT REPEAT 3350..3387
FT /note="Plectin 13"
FT REPEAT 3388..3425
FT /note="Plectin 14"
FT REPEAT 3429..3463
FT /note="Plectin 15"
FT REPEAT 3609..3646
FT /note="Plectin 16"
FT REPEAT 3647..3684
FT /note="Plectin 17"
FT REPEAT 3685..3722
FT /note="Plectin 18"
FT REPEAT 3723..3760
FT /note="Plectin 19"
FT REPEAT 3764..3797
FT /note="Plectin 20"
FT REPEAT 3800..3834
FT /note="Plectin 21"
FT REPEAT 3852..3889
FT /note="Plectin 22"
FT REPEAT 3890..3927
FT /note="Plectin 23"
FT REPEAT 3928..3965
FT /note="Plectin 24"
FT REPEAT 3966..4003
FT /note="Plectin 25"
FT REPEAT 4007..4041
FT /note="Plectin 26"
FT REPEAT 4043..4094
FT /note="Plectin 27"
FT REPEAT 4197..4234
FT /note="Plectin 28"
FT REPEAT 4235..4272
FT /note="Plectin 29"
FT REPEAT 4273..4310
FT /note="Plectin 30"
FT REPEAT 4311..4348
FT /note="Plectin 31"
FT REPEAT 4349..4386
FT /note="Plectin 32"
FT REGION <1..1259
FT /note="Globular 1"
FT REGION <1..192
FT /note="Actin-binding"
FT REGION 1260..2544
FT /note="Central fibrous rod domain"
FT REGION 1274..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1881..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1950..1971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2003..2098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2457..2476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2545..4473
FT /note="Globular 2"
FT REGION 4039..4089
FT /note="Binding to intermediate filaments"
FT /evidence="ECO:0000250"
FT REGION 4400..4473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4414..4429
FT /note="4 X 4 AA tandem repeats of G-S-R-X"
FT COILED 1258..2548
FT /evidence="ECO:0000255"
FT COMPBIAS 1586..1616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2003..2048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2060..2074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4400..4454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 1514
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 2425
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30427"
FT MOD_RES 2591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 2675
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 2822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2842
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2880
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3579
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3819
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 3843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4182
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30427"
FT MOD_RES 4200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4328
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:8626512"
FT MOD_RES 4396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4404
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4416
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4429
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT MOD_RES 4464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15149"
FT NON_TER 1
SQ SEQUENCE 4473 AA; 509020 MW; E144615D361E3484 CRC64;
DGHNLISLLE VLSGDSLPRE KGRMRFHKLQ NVQIALDYLR HRQVKLVNIR NDDIADGNPK
LTLGLIWTII LHFQISDIQV SGQSEDMTAK EKLLLWSQRM VEGYQGLRCD NFTTSWRDGR
LFNAIIHRHK PMLIDMNKVY RQTNLENLDQ AFSVAERDLG VTRLLDPEDV DVPQPDEKSI
ITYVSSLYDA MPRVPGAQNG VRANELQLRW QEYRELVLLL LQWIRHHTAA FEERKFPSSF
EEIEILWCQF LKFKETELPA KEADKSRSKG IYQSLEGAVQ AGQLQIPPGF HPLDVEKEWG
KLHVAILERE KQLRGEFERL ECLQRIVSKL QMEAGLCEEQ LNQADSLLQS DIRLLASGKV
AQRAGEVERD LDKADGMIRL LFNDVQTLKD GRHPQGEQMY RRVYRLHERL VAIRTEYNLR
LKAGVAAPVT QVTVQSTQRR PELEDSTLRY LQDLLAWVEE NQRRIDSAEW GVDLPSVEAQ
LGSHRGMHQS IEEFRAKIER ARNDESQLSP ATRGAYRECL GRLDLQYAKL LNSSKARLRS
LESLHGFVAA ATKELMWLNE KEEEEVGFDW SDRNTNMAAK KESYSALMRE LEMKEKKIKE
TQNTGDRLLR EDHHARPTVE SFQAALQTQW SWMLQLCCCI EAHLKENTAY FQFFSDVREA
EEQLQKLQET MRREYSCDRS ITVTRLEDLL QDAQDEREQL NEYKGHLSGL AKRAKAIVQL
KPRNPAHPVR GHVPLMAVCD YKQVEVTVHK GDQCQLVGPA QPSHWKVLRG PSSEAAVPSV
CFLVPPPNQE AQEAVARLEA QHQALVTLWH QLHVDMKSLL AWQNLSRDIQ LIRSWSLVTF
RTLKPEEQRQ ALRNLELHYQ AFLRDSQDAG GFGPEDRLVA EREYGSCSRH YQQLLQSLEQ
GEQEESRCQR CISELKDIRL QLEACETRTV HRLRLPLDKE PARECAQRIA EQQKAQAEVE
GLGKGVARLS AEAEKVLALP EPSPAAPTLR SELELTLGKL EQVRSLSAIY LEKLKTISLV
IRSTQGAEEV LKAHEEQLKE AQAVPATLQE LEATKASLKK LRAQAEAQQP VFDTLRDELR
GAQEVGERLQ QRHGERDVEV ERWRERVNQL LERWQAVLAQ IDVRQRELEQ LGRQLRYYRE
SADPLSSWLQ DAKRRQEQIQ AVPIPNSQAA REQLRQEKAL LEEIERHGEK VEECQKFAKQ
YINAIKDYEL QLVTYKAQLE PVASPAKKPK VQSGSESVIQ EYVDLRTRYS ELTTLTSQYI
KFISETLRRM EEEERLAEQQ RAEERERLAE GEAALEKQRQ LAEAHAQAKA QAELEAQELQ
RRMQEEVARR EEAAVNAQQQ KRSIQEELQH LRQSSEAEIQ AKAQQVEAAE RSRMRIEEEI
RVVRLQLETT ERQRGGAEGE LQALRARAEE AEAQKRQAQE EAERLRRQVQ DESQRKRQAE
AELALRVKAQ AEAAQEKQRA LQALEELRLQ AEEAERRLRQ AQAERARQVQ VALETAQRSA
EVELQSKRAS FAEKTAQLER TLQEEHVTVT QLREKAERRA QQQAEAERAR EEAERELERW
QLKANEALRL RLQAEEVAQQ RSLAQADAEK QKEEAEREAR RRGKAEEQAV RQRELAEQEL
EKQRQLAEGT AQQRLAAEQE LIRLRAETEQ GEQQRQLLEE ELARLQREAT AATHKRQELE
AELAKVRAEM EVLLASKARA EEESRSTSEK SKQRLEAEAD RFRELAEEAA RLRALAEEAK
RQRQLAEEDA ARQRAEAERV LTEKLAAISE ATRLKTEAEI ALKEKEAENE RLRRLAEDEA
FQRRRLEEQA ALHKADIEER LAQLRKASES ELERQKGLVE DTLRQRRQVE EEILALKVSF
EKAAAGKAEL ELELGRIRSS AEDTMRSKEQ AEQEAARQRQ LAAEEEQRRR EAEERVQKSL
AAEEEAARQR KAALEEVERL KAKVEEARRL RERAEQESAR QLQLAQEAAQ KRLQAEEKAH
AFVVQQREEE LQQTLQQEQS MLERLRGEAE AARRAAEEAE EAREQAEREA AQSRKQVEEA
ERLKQSAEEQ AQARAQAQAA AEKLRKEAEQ EAARRAQAEQ AALKQKQAAD AEMEKHKKFA
EQTLRQKAQV EQELTTLRLQ LEETDHQKSI LDEELQRLKA EVTEAARQRS QVEEELFSVR
VQMEELGKLK ARIEAENRAL ILRDKDNTQR FLEEEAEKMK QVAEEAARLS VAAQEAARLR
QLAEEDLAQQ RALAEKMLKE KMQAVQEATR LKAEAELLQQ QKELAQEQAR RLQEDKEQMA
QQLVEETQGF QRTLEVERQR QLEMSAEAER LKLRMAEMSR AQARAEEDAQ RFRKQAEEIG
EKLHRTELAT QEKVTLVQTL EIQRQQSDHD AERLREAIAE LEREKEKLKQ EAKLLQLKSE
EMQTVQQEQI LQETQALQKS FLSEKDSLLQ RERFIEQEKA KLEQLFQDEV AKAQQLREEQ
QRQQRQMEQE KQELVASMEE ARRRQCEAEE AVRRKQEELQ HLELQRQQQE KLLAEENQRL
RERLQRLEEE HRAALAHSEE IAATQAAAAK ALPNGRDALD GPSMEVEPEH AFEGLRQKVP
ALQLREAGIL SAEELQRLEQ GHTTVAELSQ REDVRQYLQG RSSIAGLLLK PTDEKLSVYT
ALQRQLLSPG TALILLEAQA ASGFLLDPVR NRRLTVNEPV KEGVVGPELH HKLLSAERAV
TGYKDPYTGE QISLFQAMKK DLLVRDHAIR LLEAQIATGG IIDTVHSHRV PVDVAYQRGY
FDEEMSRILA DPGDDTKGFF DPNTHENLTY LQLLERCVED PETGLHLLPL TDKAAKGGEL
VYTDTEARDV FEKATVSAPF GKFQGKTVTI WEIINSEYFT AEQRRDLLRQ FRTGRITVEK
IIKIVITVVE EQERKGQLCF EGLRALVPAA ELLESGVISH ELYQQLQRGE RSVREVAEAD
SVRRALRGAS VIAGVWLEEA GQKLSIYEAL KKDLLQPDVA VALLEAQAGT GHIIDPATSA
RLTVDEAVRA GLVGPELHEK LLSAEKAVTG YRDPYSGQSV SLFQALKKGL IPREQGLRLL
DAQLSTGGMV DPSKSHRVPL DVAYARGYLD KETNRALTSP RNDARVYLDP SSQEPATYSQ
LQQRCRADQL TGLSLLPVSE KAVRARQEEV YSELQARETL EKARVEVPVG GFKGRTMTVW
ELISSEYFTQ EQRQELLRQF RTGKVTVEKV IRIVITIVEE VETQRQERLS FSGLRAPVPA
SELLAAKILS RAQFDQLKEG KTSVKDLSEV GSVRTLLQGS GCLAGVYLED SKEKVTIYEA
MRRGLLRPST ATLLLEAQAA TGFLVDPVRN QRLYVHEAVK AGVVGPELHE KLLSAEKAVT
GYKDPYSGTT ISLFQAMKKG LVLREHAIRL LEAQIATGGI IDPVHSHRLP VDVAYQRGYF
DEEMSRILAD PSDDTKGFFD PNTHENLTYL QLLERCVEDP ETGLRLLPLK GAEKTEVVET
TQVYTEEETR RAFEETQIDI PGGGSHGGSS MSLWEVMQSD MIPEDQRARL MADFQAGRVT
KERMIIIIIE IIEKTEIIRQ QNLASYDYVR RRLTAEDLYE ARIISLETYN LFREGTKSLR
EVLEMESAWR YLYGTGSVAG VYLPGSRQTL TIYQALKKGL LSAEVARLLL EAQAATGFLL
DPVKGERLTV DEAVRKGLVG PELHDRLLSA ERAVTGYRDP YTEQTISLFQ AMKKELIPAE
EALRLLDAQL ATGGIVDPRL GFHLPLEVAY QRGYLNKDTH DQLSEPSEVR SYVDPSTDER
LSYTQLLKRC RRDDGSGQML LPLSDARRLT FRGLRKQITV EELVRSQVMD EATALQLQEG
LTSIEEVTKT LQKFLEGTSC IAGVFVDATK ERLSVYQAMK KGIIRPGTAF ELLEAQAATG
YVIDPIKGLK LTVEEAVRMG IVGPEFKDRL LSAERAVTGY KDPYSGKLIS LFQAMKKGLI
LKDHGIRLLE AQIATGGIID PEESHRLPVE VAYKRGLFDE EMNEILTDPS DDTKGFFDPN
TEENLTYLQL MERCITDPQT GLRLLPLKEK KRERKTSSKS SVRKRRVVIV DPETSKEMSV
YEAYRKGLID HQTYLELSEQ ECEWEEITIS SSDGVVKSMI IDRRSGRQYD IDDAITENLI
DRSALDQYRA GTLSITEFAD MLSGNAGGFR SRSSSVGSSS SYPISPAVSR TQLASWSDPT
EETGPVAGIL DTETLEKVSI TEAMHRNLVD NITGQRLLEA QACTGGIIDP STGERFPVTE
AVNKGLVDKI MVDRINLAQK AFCGFEDPRT KTKMSAAQAL KKGWLYYEAG QRFLEVQYLT
GGLIEPDTPG RVPLDEALQR GTVDARTAQK LRDVSAYSKY LTCPKTKLKI SYKDALDRSM
VEEGTGLRLL EAAAQSSKGY YSPYSVSGSG STTGSRTGSR TGSRAGSRRG SFDATGSGFS
MTFSSSSYSS SGYGRRYASG PPASLGGPES AVA
