ID A0A3Q7TD44_VULVU Unreviewed; 3557 AA.
AC A0A3Q7TD44;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN Name=DMD {ECO:0000313|RefSeq:XP_025853200.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025853200.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025853200.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025853200.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025853200.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037032}.
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|PIRNR:PIRNR002341}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR RefSeq; XP_025853200.1; XM_025997415.1.
DR STRING; 9627.ENSVVUP00000010270; -.
DR OrthoDB; 2880153at2759; -.
DR Proteomes; UP000286640; 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; 11.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 17.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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; 1.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 16.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00150; SPEC; 22.
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; PS50021; CH; 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 4: Predicted;
KW Actin-binding {ECO:0000256|PIRNR:PIRNR002341};
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|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|PIRNR:PIRNR002341};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
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 11..117
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2927..2960
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3180..3236
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 187..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3400..3426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3472..3557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 627..661
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1069..1099
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1791..1818
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2068..2098
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2375..2419
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2794..2828
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 3474..3545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3557 AA; 411124 MW; 2878249805DB57FB CRC64;
MKNIMAGLQQ TNSEKILLSW VRQSTRNYPQ VNVINFTTSW SDGLALNALI HSHRPDLFDW
NSVVCQQSAT QRLEHAFNIA KYQLGIEKLL DPEDVATTYP DKKSILMYIT SLFQVLPQQV
SIEAIQEVEM LPRPSKVTRE EHFQLHHQMH YSQQITVSLA QGYERAPSSP KPRFKSYAYT
QAAYVTTSDP TRSPLPSQRL ETPEDKSFGR SLTETEVNLD SYQTALEEVL SWLLSAEDAL
QAQGEISNDV EEVKEQFHTH EGYMMDLTSH QGRVGNVLQL GSQLIGTGKL SEDEETEVQE
QMNLLNSRWE CLRVASMEKQ SNLHKVLMDL QNQQLKELND WLTKTEERTR KMEKEPLGPD
IEHLKRQVQQ HKVLQEDLEQ EQVRVNSLTH MVVVVDESSG DHATAALEEQ LKVLGDRWAN
ICRWTEDRWV LLQDILLKWQ RFTEEQCLFS AWLSEKEDAV NKIHTTGFKD QSEVLSSLQK
LAVLKTDLEK KKQTMDKLCS LNQDLLSALK NTVVAQKMEA WLDSFAQRWD NLVQKLEKSS
AQISQAVTTT QPSLTQTTVM ETVTMVTTRE HILVKHAQEE LPPPPPQKKR QIIVDSEIRK
RLDVDITELH SWITRSEAVL QSPEFAIYRK EGNVSDLKEK VNAIEREKAE KFRKLQDASR
SAQALVEQMV NEGVNADSIK QASEQLNSRW IEFCQLLSER LNWLEYQNNI ITFYNQLQQL
EQMTTTAENW LKTQPTTTSE PTAIKSQLKI CKDEINRLSA LQPQIERLKI QSIALKEKGQ
GPMFLDADFV AFTNHFNQVF ADVQAREKEL QTIFDSLPPM RYQETMSTIL TWIQQSETKL
SIPQVTVTEY DIMEQRLGEL QALQSSLQEQ QNGLNYLSTT VKEMSKKAPL SDISRKYQSE
FEEIEGRWKK LSSQLVEHCQ KLEEQMAKLR KIQNHIKTLK KWITEVDVFL KEEWPALGDS
EILKRQLKQC RLLVNDIQTI QPSLNSVNEG AQKMKNEAEP EFAGRLETEL RELNTQWDYM
CRQVYARKEA LKGGLDKTVS LQKDLSEMHE WMTQAEEEYL ERDFEYKTPD ELQTAVEEMK
RAKEEAQQKE AKVKLLTESV NSVIAQAPPA AQEALKKELD TLTTNYQWLC TRLNGKCKTL
EEVWACWHEL LSYLEKANKW LSEVEAKLKT TENISGGAEE IAEVLDSLEN LMQHSEDNPN
QIRILAQTLT DGGVMDELIN EELETFNSRW RELHEEAVRR QKLLEQSIQS AQEIEKSLHL
IQESLSSIDK QLAAYIADKV DAAQMPQEAQ KIQSDLTSHE ISLEEMKKHN QGKETAQRVL
SQIDVAQKKL QDVSMKFRLF QKPANFEQRL QESKMILDEV KMHLPALETK SVEQEVVQSQ
LNHCVNLYKS LSEVKSEVEM VIKTGRQIVQ KKQTENPKEL DERVTALKLH YNELGAKVTE
RKQQLEKCLK LSRKMRKEMN ALTEWLAATD MELTKRSAVE GMPSNLDSEV AWGKATQKEI
EKQKVHLKSV TEVGEALKTV LGKKEMLVED KLSLLNSNWI AVTSRAEEWL NLLLEYQKHM
ENFDQNVDYI TNWIIQADAL LDESEKKKPQ QKEDILKRLK AEMNDMRPKV DSTRDQAANL
MANRGDHCRK VVEPKISELN HRFAAISHRI KTGKASIPLK ELEQFNSDIQ KLLEPLEAEI
QQGVNLKEED FNKDMSEDNE GTVKELLQRG DNLQQRITDE RKREEIKIKQ QLLQTKHNAL
KDLRSQRRKK ALEISHQWYQ YKRQADDLLK CLDDIEKKLA SLPEPRDERK IKEIDRELQK
KKEELNAVRR QAEGLSEDGA AMAVEPTQIQ LSKRWREIES KFAQFRRLNF AQIHTVHEES
VVAMTEDMPL EISYVPSTYL TEITHVSQAL SEVEELLNAP DLCAQDFEDL FKQEESLKNI
KDSLQQISGR IDIIHNKKTA ALHSATPAER AKLQEALSRL DFQWERVNNM YKDRQGRFDR
SVEKWRRFHY DMKILNQWLT EAEQFLKKTQ IPENWEHAKY KWYLKELQDG IGQRQTVVRV
LNATGEEIIQ QSSKTDASIL QEKLGSLNLR WQEVCKQLAE RKKRLEEQKN ILSEFQRDVN
EFVLWLEEAD NVANIPLEPG NEQQLKEKLE QVKLLAEELP LRQGILKQLN ETGGTVLVSA
PLSPEEQDKL ENKLKQTNLQ WIKVSRNLPE KQEEIEAHVK DLGQLEEQLN HLLLWLSPIR
NQLEIYNQPN QTGPFDIKEI EVAVQAKQPD VEGILSKGQH LYKEKPATQP AKRKLEDLSS
DWKVVTQLLQ ELRAKQPGPA PGLTTVRAPP SQTVTLVTQP AVAKETAISK LEMPSSLLLE
VPALADFNRA WTELTDWLSL LDRVIKSQRV MVGDLEDINE MIIKQKATLQ DLEQRRPQLE
ELITAAQNLK NKTSNQEART IITDRIERIQ SQWDEVQEHL QNRRQQLNEM LKDSTQWLEA
KEEAEQVLGQ ARAKLESWKE APYTVDAIQK KITETKQLAK DLRQWQINVD VANDLALKLL
RDYSADDTRK VHMITENINA SWASIHKRLS EREAALEETH RLLQQFPLDL EKFLAWLTEA
ETTANVLQDA THKERLLEDS KGVRELMKQW QDLQGEIEAH TDIYHNLDEN GQKVLRSLEG
SDDAALLQRR LDNMNFKWSE LRKKSLNIRS HLEASSDQWK RLHLSLQELL VWLQLKDDEL
SRQAPIGGDF PAVQKQNDVH RAFKRELKTK EPVIMSTLET VRIFLTEQPL EGLEKLYQEP
RELPPEERAQ NVTRLLRKQA EEVNTQWEKL NVHSADWQRK IDEALERLQE LQEATDELDL
KLRQAEVIKG SWQPVGDLLI DSLQDHLEKV KALRGEITPL KENVSYVNDL ARQLTTLGIQ
LSPYNLNTLE DLNTRWKLLQ VAIEDRIRQL HEAHRDFGPA SQHFLSTSVQ GPWERAISPN
KVPYYINHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA
ACDALDQHNL KQNDQPMDIL QVINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT
GRTGRIRVLS FKTGIISLCK 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 LNQDSPLSQP
RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK QQHEHKGLSP LPSPPEMMPT
SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQAEAKVNG
TTVSSPSTSL QRSDSSQPML LRVVGSQTSE SMGEEDLLSP PQDTSTGLEE VMEQLNHSFP
SSRGRNTPGK PMREDTM
//
