ID A0A1D1VB69_RAMVA Unreviewed; 2679 AA.
AC A0A1D1VB69;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dystrophin {ECO:0008006|Google:ProtNLM};
GN Name=RvY_09254-1 {ECO:0000313|EMBL:GAU98055.1};
GN Synonyms=RvY_09254.1 {ECO:0000313|EMBL:GAU98055.1};
GN ORFNames=RvY_09254 {ECO:0000313|EMBL:GAU98055.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU98055.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAU98055.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU98055.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAU98055.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDGG01000004; GAU98055.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1VB69; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:UniProt.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
DR CDD; cd16242; EFh_DMD_like; 1.
DR CDD; cd00176; SPEC; 4.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 8.
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; 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:SF14; DYSTROPHIN-1; 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; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 9.
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; 10.
DR SUPFAM; SSF51045; WW domain; 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 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 51..155
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 169..274
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2053..2086
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 2308..2364
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2588..2633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1385..1484
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1926..1953
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2007..2034
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2504..2588
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2596..2633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2679 AA; 305457 MW; 67B18E4A33B9E490 CRC64;
MPLVPGLTMS VRESKRRQKG KEELPKIDPS EEVADDVIKD IVKGRTDEQE RIQQKVFGRW
INSRFAKANS PLRVDDLFQD FRTGVTLAAL VELITGIKVP VEKGRTRFAC ASNISSALEV
LQNEIKLVSV STEDIEEGNS KLTLALTWSI IQHYYVKRLG STVSDLRVNN LEKTLLCWCQ
LATKGYAHVD VKNLHTSWTD GLAFNAVIHK YREDLFKYSD LLSNTAKVNL RHAFDLAAQH
LDVPRLLEPE DLLQSYVDQK SIVIYLLCLL ESLPHESMEM NAVTSVSMLE TNPAAGDADS
NRTYQSSAEA VLAWLLAAEE KLDRSEISES LEETTQLWND HEALLGEISM QESVVQKVLD
HGAKLLQRIK SQPKQSAEVE NSLTLLMERW ENLRSKATER SHLLQRMISV LQQEHLKEVD
SWLQDTEKRV NSLKANTTSI ESMDAQLREL SKLQDDLEKQ LLVMNRLLRV LFVGEISENE
ALESKLLGFR QRWDEICHWT EFQWAFVQRI RNTYDEFSKL CAACGEWIAG RIELLQSLPR
LTDERVQWVQ RNLDMLQELH DQMADQQESI QDLQEKSEVL LGYFTPQTSV GMQIRHREEK
ISSDWNILVD LLEVLTADVD LRFEKADELR TSKLRQSKRY SDHVDTATVF TQSSEETEPK
TKKARQEEED EGVLENCNVL IDWLEEQSEL LDKQNGGSLL TSQTIKDEIK AKELEYNSVR
MLAETVIAEK RKMNVPFEEV ENKLNELAAA WSRAEAWNMD ADNDIQMKDD ELTMNSNLEV
LKDVLISCQS AVDRLTTDKD PLPGRIEQDL TDCKDRLHLI ELNSERFKET AGLVDKVSND
LRTSPTSSTD IESSWAEVAK RWQVVKQSLG DLEKRLSDFK ENQPVRLFLA EIESLLAWTN
GIHQSLMEEP PLRPTYLDRM EELLRRYQSI QNAVNQHQQS LELANLPPKQ LVEKLSGTNY
QMSLLDLNAK WKDILQYLQH NTEEMTKWIE NLRDFQVDVE GLKQWMADVN SFLDIDTESV
DDPQAFSALQ EQFQGLEEDI KALSPTTDKL MEAGRLFLRS SHEDFVEDMR GILQDVEAQW
SATCARASRQ MQAVPVIAAQ RNMAVGSPAR AVGKMTPVTD RVKHIQEEMR SIENMNDLRR
LSHETKEAMK TAQLYLAPAT GRTPTDSELA LVKQCLDDLH SYESTLNRHQ EMWKDLSGFL
KEAEDWVVVA EKKALDVEKA FSDTQRRKQL QELTAYMGAQ NTDKYVSIAD LAEQFTAAGV
LVSLVRTEVD KMRQRLSSLS KQVSDLQHMN SADGTDSRSE DVSRAEIAAH TTLFDSLEPV
DRLLNELQKK LPSMDLKQFD SATIKTQLED CVMLYKKLSE IKAEVESLIK QGREAVESDP
TRPENESLSR KLDSMKTQYN QLGAQVTAAK AELDNGFKLV KKAEKELDLF RLAMDEMEAA
LAELDKITDQ LEYESTIEDI KSAIKEREET LNNLRSSHQQ MRELAMKSNV PGFELKYSAQ
MQRWTKLQTH LKSLKTIEKD KMHKPMSVAR EAFFSDMMTV QVASAGSTKT SESPTISTEN
KPKQDHQQEV QRKIDEKRQM ITSTHLRAFA ENKRTEEQIE RILQLDGQIQ QLYSADVEIE
KKLDGLFTEP LDLKQFNARL QVLEGIQRDL PARDHDKQKV VDQLSTLKSD LRGSADVSHL
VSLEQDITQR TTEVHDRSAK SRKILEDLQL YYKLAEEDLL VWLPKAEAVA TELATSSKRG
TFSNERYRRL VEERDSRIPH FDTAVRSAHN AVAEKESEPV GSTLKRDLAS LTLRWDNLNT
AISGIKETQI EDRLDVESYM ASLLEAEKWV MRKKDELMTM RPSGDRAFLG KLQDYHHLFR
AQLEREKPNI DSLLARGKLL EEQLTTDPRK SAHGKSTMGD LSEKLKSLSA SWQSLFQQSD
ALQVETEGVT EELERLLELC DAAREKLENL QRDTEKWDLP DDVNVAELPK KIEDSKKFKS
KVDAQAAKLE EVNSLAARIQ RTHAGLSEEV VRSVAHLNER KQDLQDKVDN RLEKLLSATE
DVTSSENQHF LATSVDEPWE RRVGPNRTPY YINHSEQKTQ WDHPRMTDLM SALLEVNNIR
FSAYRTATKL RLMQKKLHLD LLPLNTASEI FDKCGLRAQN DTVLDCSQAV TCLMAIYSYI
DAQHPNRINF SLSIDVCLNW LLNCHDPERT GQISVLTFKV SIVILCQGEL NAKYRYLFRL
ISDANGFADQ KRVGQLLYSC IHIPRLLGEV AAFGGTDPQP SIDSCFKFSK TNGLNIQQKE
FLAWLNREPQ AVVWLSVLHR LIAAEGSRHP AKCNACRQFP IIGLRYRCLK CFNFDLCQNC
FFTGQRSKNH KISHPMQEYC FPATSGEDMR DFKRVLKNKL RSRESLTGSS KSLGYLPVQQ
TSARGSDYEK SATLTSLAAK GSIGSNDAAD FTQSRLVYSV RQSLFKLMTY KDLMVVRCRI
IEFEGSRGAS SPEADEEHTL ITRYCNTLSA PAHDFSQMPD QILRAVDKEE KEEMEDYLRQ
LQEDHDKLIV ELESVKQLHD EIPADDLLAE ASMLRDDKGR LEARMRVLKD HNQQLDSQLQ
RIKHLLEETP ERVPASPVPS NYSNGRATPA DNLITKGSSS VANGSSPLPT KKAARQETYS
VGQLFHAAGS LNVAVGSLVT VMNEEEQAAL NKPSAVSGS
//