ID A0A2Y9SM04_PHYMC Unreviewed; 3432 AA.
AC A0A2Y9SM04;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Utrophin isoform X3 {ECO:0000313|RefSeq:XP_023978467.1, ECO:0000313|RefSeq:XP_023978468.1};
GN Name=UTRN {ECO:0000313|RefSeq:XP_023978467.1,
GN ECO:0000313|RefSeq:XP_023978468.1, ECO:0000313|RefSeq:XP_023978469.1,
GN ECO:0000313|RefSeq:XP_023978470.1, ECO:0000313|RefSeq:XP_023978471.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023978467.1};
RN [1] {ECO:0000313|RefSeq:XP_023978467.1, ECO:0000313|RefSeq:XP_023978468.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023978467.1,
RC ECO:0000313|RefSeq:XP_023978468.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR002341}.
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DR RefSeq; XP_023978467.1; XM_024122699.3.
DR RefSeq; XP_023978468.1; XM_024122700.3.
DR RefSeq; XP_023978469.1; XM_024122701.3.
DR RefSeq; XP_023978470.1; XM_024122702.3.
DR RefSeq; XP_023978471.1; XM_024122703.3.
DR Proteomes; UP000248484; Chromosome 10.
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-UniRule.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd21232; CH_UTRN_rpt1; 1.
DR CDD; cd21234; CH_UTRN_rpt2; 1.
DR CDD; cd16247; EFh_UTRO; 1.
DR CDD; cd00176; SPEC; 9.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 14.
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; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR PANTHER; PTHR12268:SF26; UTROPHIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 10.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 3.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 20.
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; 14.
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 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:UP000248484};
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 31..135
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 150..255
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2812..2845
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3065..3121
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3289..3309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3356..3388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1101..1190
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1690..1750
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2112..2139
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2686..2713
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3253..3287
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 3356..3380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3432 AA; 394250 MW; 112BC57B004ABDE8 CRC64;
MAKYGEHEAR ADDGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPISDMFTDL
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVDLVNI GGTDIVDGNH
KLTLGLLWSI ILHWQVKDVM KDIMSDLQQT NSEKILLSWV RQSTRPYSQV NVLNFTTSWT
DGLAFNAVLH RHKPDLFSWD RVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK
KSIIMYLTSL FEVLPQQVTI DAIREVETLP RKYKKECEEG EINMQVQSSA PEEEQEGPRA
ETPSTVTEVD MDLDSYQIAL EEVLTWLLSA EDTFQEQDDI SDDVEEVKDQ FATHEAFMME
LTAHQSSVGN VLQAGNQLIT QGTLSDEEEF EIQEQMTLLN ARWEALRVAS MDRQSRLHDV
LMELQRKQLQ QLSAWLTLTE ERIQKMETCP LDDDLKSLQK LLEDHKSLQN DLEAEQVKVN
SLTHMVVIVD ENSGESATAI LEDQLQKLGE RWTAVCRWTE ERWNRLQEIN ILWQELLEEQ
CLLKAWLTEK GEALNKVQTS NFKDQKELSV SVRRLAILKE DMEMKRQVLD QLSEIGQDVG
QLLDNPKASK KINSDSEELT QRWDSLVQRL EDSSNQVTQA VAKLGMSQIP QKDLLETVRL
REQVTTKRSK QELPPPPPPK KRQIPVDLET KKRFDAISAE LLNWILKSKT AIQATEIKEY
KKMQETSEMK KKLKGLEKEQ MERRSRLDEL NQTGQILLEQ MGKEGLPTEE IKNVLEKVVS
EWKNISQHLE DLARKIQLQE DINAYCKHLD ELEKTIKTKE EWVKHTPFSE SPQQSLPSLK
DSCQQELTDL RSHHPKIEML RASCSALKSQ PSAPDFVQRD FESFVGRYQA VQQDLEGRHQ
QLENELKSRP GREYLETLKT LTDLLNDSEN KAQTSLNVLN DLAKVEKALQ EEKALDEILE
NQKPVLHKLA EETKALEKNV SPDVEKLYKQ EFDDVQGKWN RLKAKVSKDL HLLEEITPKL
RTFEADSKVI EKWMDGVKDF LMKEQAVQGD AEGLQRQLDQ CSAFVNEIET IESSLKDMKE
IEANLRSSPV AGIKTWMQTK LADYQTRLEK CSKEITIQKN RLSESQEKVV NLKKDLAEMQ
EWMTQAEEDY LERDFEYKSP EELESAVEEM KRAKEDVLQK EVRVKILKDN IKLLAAKVPS
GGQELTSELN VVLENYQLLC NRIRGKCHTL EEVWSCWIEL LHYLDLETTW LNTLEERMKS
TEALPEKTDA VSEALESLES VLRHPADNRT QIRELGQTLI DGGILDDIIS EKLEVFNSRY
EELSHLAESK QISLEKQLQV LRETDHMLQV LQESLGELDK QLTTYLTDRI DAFQVPQEAQ
KIQAEISAHE LTLEELRRNT RSQPPTSPEG RRGGSQMDVL QRKLREVSTK FQLFQKPANF
EQRMLDCKRV LEGVKAELHV LDVKDVDPDV IQTHLDKCMK LYKILSEVKL EVETVIKTGR
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLARKMK KEAASLSEWL
SVTETELVQK STSESLLGDL DTEISWAKNI LKDLEKRKAD LNTITESSAA LQNLIEGSEP
VLEEKLCVLN AGWSRVRTWT EDWCNTLMNH QNQLEIFDGN VAHISTWLYQ AEALLDEIEK
KPASKREEIV KRLLSELDDA NLQVENVRDQ AVVLMNARGG SSKELVEPKL AELNRNFEKV
SQHIKSAKLL IGQEPLSYQY LVTTEAFEAG VPFSDFEKLE NDIENMLKVT EKRLESSDED
EKMDEERAQI EEVLQRGEQM LHQPMEDNKK EKIRLQLLLL HTRYNKTKAI PIQQRTGHLP
SGISSPPLPT DYLVEINKVL LSMDDVELSL NTPELSSVVY EDFSFQEDSL KTIKDQLDKL
GEQIAIIHEK QPDVILEASG PEAIQIRDTL TQLNAKWDRI NRMYNDHKGY FDRAVEEWRQ
FHCDLNDLTQ WITEAEELLA DTFAPDGGLD LEKARIHQQE LEEGIGSHQP SFAALNRTGD
GIVQKLSPTD GSFLKDKLAS LNQRWGAIAA EVKDRRPRLK GESKQVMDYR KRLDEIICWL
TKAENAVQKR STTELEENLQ ELTDLIQEMD DQAEKLKWLN RTELEMLSDK SLSLHEREKI
SESLRTVNST WNKICREVPS ALKERIQEPC SVAQTRIAAH PSVQKVVLAS SASDIPVQSP
RTSEISVPAD LDKTITELAD WLVLIDQMLK SNIVTVGDVE EINKTISRMK ITKADLEQRH
PQLDYVFTLA QNLKNKASSS DVRTAITEKL EKVKNQWDST QHGVELRQQQ LEDMIIDSLQ
WDDHREETEE LMRKYEARLY ILQQARRDPL IKQISDNQML LQELAPGAGI VMAFDNVLQK
LLEEYGSDDT RNVKETTEYL KTSWINLKQS IADRQSALEG ELRTVQASRR DLENFLKWIQ
EAETTVNVLA DASQRENALQ DAVLARELTQ QMQDIQAEID AHSDIFKSLD GNRQKMVKAL
GNSEEATMLQ HRLDDMNQRW NDLKAKSASI RAHLEASAEK WNRLLTSLEE LIKWLNMKDE
ELRKQMPIGG DVPALQLQYD HCKALRRELK EKEYSVLNAI DQARVFLADQ PIEAPEEPRR
NLQSKTELTP EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM
DDLDADLKEA EAVRNGWKPV GDLLIDSLQD HIEKTMAFRE EIAPINLKVK TVNDLSSQLS
PLDLHPSLKM SRQLDDLNMR WKLFQVSVDD HLKQLQEAHR DFGPSSQHFL STSVQLPWQR
SISHNKVPYY INHQTQTTSW DHPKMTELFQ SLADLNNVRF SAYRTAIKIR RLQKALCLDL
LELNTTNEVF TQHKLNQNDQ LLSVPDVINC LTTIYDGLEQ MHKNLVNVPL CVDMCLNWLL
NVYDTGRTGK IRVQSLKIGL ISLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ
IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKEFVD WMRLEPQSMV WLPVLHRVAA
AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS GRTAKGHKLH YPMVEYCIPT
TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG YLPVQTVLEG DNLETPITLI SMWPEHYDPS
QSPQLFHDDT HSRIEQYATR LAQMERTNGS FLTDSSSTTG SVEDEHALIQ QYCQTLGGES
PVSQPQSPAQ ILKSVEREER GELERIIADL EEEQRNLQVE YKQLKEQHLR RGLPVGSPPD
SVVSPHHTSE DSELIAEAKL LRQHKGRLEA RMQILEDHNK QLESQLHRLR QLLEQPESDS
QINGVSPWAS PQQSALNYSL DPDPGPQFHQ AAAEDLLAPP HDTSTDLTEV MEQINSTFPS
CCPNLPSRPQ AM
//
