ID A0A3Q0G8K4_ALLSI Unreviewed; 3635 AA.
AC A0A3Q0G8K4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN Name=DMD {ECO:0000313|RefSeq:XP_025055996.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025055996.1};
RN [1] {ECO:0000313|RefSeq:XP_025055996.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in anchoring the cytoskeleton to the plasma
CC membrane. {ECO:0000256|PIRNR:PIRNR002341}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR002341}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR RefSeq; XP_025055996.1; XM_025200211.1.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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 CDD; cd21233; CH_DMD_rpt2; 1.
DR CDD; cd16246; EFh_DMD; 1.
DR CDD; cd00176; SPEC; 12.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 16.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
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 PANTHER; PTHR12268:SF25; DYSTROPHIN; 1.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
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; 21.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 17.
DR SUPFAM; SSF51045; WW domain; 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 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|PIRNR:PIRNR002341}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR002341}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR002341};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR002341};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002341};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|PIRNR:PIRNR002341};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|PIRNR:PIRNR002341};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1..98
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 113..219
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2987..3020
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3240..3296
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 3460..3483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3532..3557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 416..446
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 682..727
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1123..1153
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1478..1512
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1713..1743
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1845..1872
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2123..2150
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2449..2479
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2514..2575
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2854..2888
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 3534..3557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3635 AA; 420065 MW; 7BD4BDBCCA69D25F CRC64;
MCTEQEYFSF FGRHHIEDLF TDFRDGRRLL ELLEGLTGQK LAKEKGSTRV HALNNVNKAL
QVLQKNNVDL VNIGSTDIVD GNHKLTLGLI WSIILHWQVK DVMKNIMAGL QQTNSEKILL
SWVRQSTRSY PQVNVINFTS SWSDGLAFNA LIHSHRPDLF DWNSLASQQS VIQRLDHAFN
VAKRHLGIEK LLDPEDIATA YPDKKSILMY VTSLFQVLPQ QVTIEAIREV ETLPRQSKVT
REEHIHHQQH FSQQYLGVPE DKPFGRSLME EVDLDSYQTA LEEVLTWLLS AEDSLQAQGD
ISNDVEEVKE QFHTHEGFMM ELTAHQGRVG NVLQVGSQLI TAGKLSEDEE NEIQEQMNLL
NSRWENLRVA SMEKQSNLHK ILMDLQNQQL TQLTEWLAKT EERTKKVESE PLGPDLEDLK
RQIEEHKALQ EDLEQEQVKV NSLTHMVVVV DESSGDKATA ALEEQLQHLG DRWAAICRWT
EDRWVLLQDI LRKWQLFAEE QCLFDAWLTE KEDAVNSVHT TGFKDQNEML TNLRTLAILK
GDLEMKRQTL NKLNSLSQEL LAAIKNKAVA QKLEGWLENF AQRWDNLVQK MESSSKQISQ
AVTTTQTSLT QTTVMETVTM VTTREQILVK HAKEELPPPP PHKKRQLVVD SESRKRFDAD
TTELHSWMTR SEVVLQSPEF AIYRKEGNLS ELQEKVNAID REKPEKYRKL QDASRSAEAL
VEQMVNEGLN AENIKQASKQ LKSRWMEFCQ LLSERLAWLE YQNNIIAFYS NLQQLEQTAI
TAENWLKAQP TPAADPTTVK TQLEKCKDQV IHLSILQPQI EQLKVQSKAL KEKEQGPMFL
DADLVAFTNH FQQVFTDIKA REKQLQTVFD SMPPAQYKET LSTILLWIQQ SEAKLSIPQV
TVTEYEIMEQ RLRELKALQS SLQEQQKGLN YLSTTVEEMS KKAPAEVSQK YRSEIEGILG
RWKKLSAQLV ENCQKLEEMM TKLQQFQNDT KTLKKWMAEV DVFLQEEWPA LGDSEALEKQ
LEQCTALVND IQTIQPSLNG VNEVGKKMRN EAEPEFASRI QTELKELNAQ WEHICQQAFA
KKAALKGGLD KTVSLRKDLS EMHEWITQAE EEYLERDFEY KTPDELQKAV EELKRAKEEA
AQKEVKVKLL TDSVNNFIAR APPAAHEALK KELDVLITNY QRLCSRLNGK CKTLEEVWAC
WQELLSYLDA ENKWLNQMES KLRATENVQG GAEEISEALD SLENLMRHPE DNRNQIRELA
QTLTDGGVLD ELINEKLEKF NTRWEELQQE AVRRQKALEQ SIQSAQEIDK TLRLIQESLS
FVDRQLTAYI ADRVDAAQVP HEAQKIQSDL ASHEISLEEM KKRNRGKDAA ERVLSQIDVA
QKKLQDVSVK FRLFQKPANF EQRLQECKRI LDEVKLQLPK LEMRSVEQEV VQSQLDHCMK
LYKSLSEVKS EVETVIKTGR QIVQKQQTEN PKDLDERLTA LKLQYNELGA RVTEKKQELE
KCLKLSRKLR KEMNALTEWL AVTDAELTKR SAVEGMPSDL DAEVAWGKAT QKEIEKRQLH
LKSITDLGEG LRPVLKGKES LVDDKLSLLN SNWIAVTSRA EEWFNLLLEY QKHMETFDQN
VANITTWMYR AEILLDESEK QKPQQKEEVL KRLKAELNDM HPKVDFVRDQ AVDLMTNCGD
HCRKVIEPKL SELNHRFAAI SQRIKSGKVF IPLKELEQFN FDIQKLLETL EAEIQQGVNL
KEEDFHKDMT EDNETTVKEL LERGDILQQR ITDERKREEI KIKQQLLQTK HNALKDLRSQ
RRKKALEISP HWYQYKRQAD DLMKCLDDIE KKLASLPEPK DEQKLKEIDG ELEKKKEELN
AVHRQAERLS KDGAAKAVEP TLIQLSKRWR DIESKFAQFR RLNYAQIQTV YEETTVVMTE
GMTMETTYMP SAYLAEILRL LKALSEVEDH LNSPALQVKN YEDLYKQEEC LKNVKDSLGR
FSGQIEVIRS KKTSALQSAT PGEAGKIQEK LSQLNFQWEK VNKMYRDRQA RFDRSVEKWR
LFHHDMKSFS QWLTETEQNL ARTQIHPGDL ASAETKQYLK ELQDGIGRQQ TVVKTLNVTG
EQIIEQSSTA DATLLKEKLG SLNFRWQEIC RQLTERRKRL EEEKNILSEL QEGLNEFAFW
LEEADRVAGI PSEPGNEEQL KDSLEKVKFR VEELPLRKGI LKRLNETGGT VLRSALLNPE
EKHKLENRLK EVNHHWIKVS KDLPEKQKEI EDLLNNLTQF EQQLSQLALW VTPVKDQLEL
YNQVGQPAAF DIKETEAAVQ DKQLNVEGIL SRGRLLYKEK PATHPLKKKL QELTVDWTAI
NHLIQELKRK PASEVLTPGQ TVTVVTQTTV TKETTISKLE MPSSLLLEVP ALADFNKAWA
ELTDWLSLLD RVIKSQIVTV GDLDDINDMI IKQKLAESIM ASDLEMATLQ DLEQRRPQLD
ELITAAQNLK NKTTNQEART IITDRIEKIQ SQWDEVQGRL QNRRQQLHEM LKDSTQWLEA
KQEAEQVLEQ AKAKLESWKE ISYTVDALKK QNAELKQFSK ELRQWQINVD VANDMALKLL
RDYSTDDTRK VQLVTDNINT TWDTINKRVS EREAALEAAL RLLQQFYLDL EKFLAWLTEA
ETTANVLQDA TRKERILEDA KGVRELMKQW QDLQTEIEAH TDIFHNLDEN GQKILRSLEG
SDDAALLQRR LDNMNFRWGE LRKKSLNIRS HLEASSDQWK RLHLSLQELL AWLQLKEDEL
KQQSPIGGDL PTVQKQNDTH RTFKRELKAK EPVIMSVLET VRIFLAEQPL EGLEKLYQEP
RELSPEERAQ NVTRLLRKQA DEVKTEWDKL NLHSADWQKK IDETLERLQE LQEVIDELDL
KLRQAEVFKG SWQPVGDLLI DSLQDHLEKV KAYRAELAPL KDNVNHVNDL AYRFPSSDIQ
LSQYNLNCLE DLNARWKLLK VAIDERIRQL HDAHRDFGPT SQHFLSTSVQ GPWERAISPN
KVPYYINHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA
ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT
GRTGRIRVLS FKTGVISLCK AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL
GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK
HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED
VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET PVTLINFWPV DSAPASSPQL
SHDDTHSRIE HYASRLAEME NSNGSYLNDS ISPNESIDDE HLLIQHYCQS LNQESPLSQP
RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK QQHDHKGLSP LPSPPEMMPI
SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQADAKVNG
TTLSSPSTSL QRSDSSQPML LRVVGSQTSE TMGEDDLLNP PQDTSTGLEE VMEQLNNSFP
STRGHNVGSL FHMADDLGRA METLVTVMTD DKVLE
//
