ID A0A3Q7TET5_VULVU Unreviewed; 3438 AA.
AC A0A3Q7TET5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Utrophin isoform X3 {ECO:0000313|RefSeq:XP_025853745.1};
GN Name=UTRN {ECO:0000313|RefSeq:XP_025853745.1};
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_025853745.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025853745.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025853745.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025853745.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR002341}.
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 RefSeq; XP_025853745.1; XM_025997960.1.
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-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; 10.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 13.
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; 9.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 3.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 19.
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; 15.
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: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 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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3277..3296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3344..3364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 883..960
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1098..1187
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1689..1716
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1903..1930
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2105..2135
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2551..2585
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2686..2713
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3240..3277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 280..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3438 AA; 395515 MW; D7C014B01B364890 CRC64;
MAKYGEHEAR PDDGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFTDL
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVDLVNI GGTDIVDGNH
KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT NSEKILLSWV RQSTRPYSQV NVLNFTTSWT
DGLAFNAVLH RHKPDLFSWD RVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK
KSIIMYLTSL FEVLPQQVTL DAIREVETLP RKYKKECEEG EISIQSSAPE EEHECPGAET
PSTVTEVDTD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEEVKEQFT THEAFMMELT
AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR WEALRVDSMN RQSRLHDVLM
ELQKKQLQQL SAWLTLTEER IQKMETCPLD DDLKSLQKLL EDHKRLQNDL EAEQVKVNSL
THMVVIVDEN SGESATAVLE DQLQKLGERW TAVCRWTEER WSRLQEINIL WQELLEEQCL
LKAWLTEKEE ALNKVQTSNF KDQKELSVSI RRLAILKEDM EMKRQALDQL SEIGQDVGQL
VDNPKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK DLLETVRVRE
QVTTKRSKQE LPPPPPPKKR QIPVDIEAKK KFDAVSAELL NFILKSKTAI QAAEIKGYKK
MQETSEMKKK LKGLEKEQTE RSPRLDELNQ TGQVLLEQMG KEGIPTEEIK NVLEKVFSEW
KDISQHLEDL ARKIQLQEDI NAYFKQLDDL EKIIKTKEEW VKHTPFSEAP QQPLPSLKDS
CQRELTDLLG LHPKIEMART YCLALKSRPL APDFVQQGFE SLLGRYQAVR QELEHRQQQL
ENELKSQPVR AYLETLKTLK NTLNDSESKA QTSLNVLNDL TKVEKALQEK KALDEILENQ
RPTLYTLAEE TKALEKTISP DVEKMYKQEF DDVQGKWNKL KVKVSKDLHL LEEVTSKLRA
FEADSKVIEK WMDGVKDFMK EQAVQRDAEG LQSQLDQCCG FVNEIETVES SLKDMKEIET
NLRSYPVAGI KTWMQTKLVD YQTQLEKFSK EIAIQKNRLS ESQEKAVNLK KDLAEMQEWM
TQAEEEYLER DFEYKSPEEL ESAVEEMKRA KEDVLQKEVR VKILKDNIML LAAKAPSGGQ
ELTSELNVVL ENYQLLCNRI RGKCHTLEEV WSCWIELLHY LDLETTWLNT LEERMKSTEA
LPEKTDAVNE ALESLESVLR HPADNRTQIR ELGQTLIDGG ILDDIISEKL EAFNNRYEEL
SHLAESKQIS LEKQLQVLRE TDHMLQVLQE SLGELDKQLT TYLTDRIDAF QVPQEAQKIQ
AEISAHELTL EELRRNIRSQ PPTSPESRNA RGGSQMDVLQ RKLREVSTKF QLFQKPANFE
QRMLDCKRVL DCVKAELHVL DVKDVDPDII QNHLDKCMKL YKTLSEVKLE VETVIKTGRH
IVQKQQTDNP KGMDEQLTSL KILYNDLGAQ VTEGKQDLER ASQLARKMKK DTASLSEWLS
VTETELVQKS TSEGLLGDLD VEISWAKNVL KDLEKRKADL NTITESSAAL QNLIEGSEPI
LEERLCVLNA GWSRVRTWTE DWCNTLMNHQ NQLEIFDGNV AHISTWLYQA EALLDEIEKK
PASKREEIVK RLISELDDAN LQVENVRDQA VVLMNARGGS SRELVEPKLA ELNRNFEKVS
QHIRSANLLI DQEPLSYQRL VTTEAFEADV LFSDLEKLES DIENMLKVVE KHLEFSGEDE
KVDEERAQIE EVLQRGEQML HQPMEDNKKE KIRLQLLLLR TRYNKTKTVP NQQRRTGQLA
PGIRLSPLPT DYLAEISKVL LSMDDAELSL NAPELSTVVY EDFSFQEDSL KNIKEQLDKL
GEQIAVIHEK QPDVILEASG TEAIQIRDTL TQLNAKWDRI NRMYNDRKSH FDRAVEEWRQ
FHCDLNDLTQ WITEAEELLA ESFAPDGGLD LEKARMHQQE LEEGISSHQP SFAALNRTGE
GIVQKLSPMD GSFLKDKLAG LNQRWNAIFA EVKDRWPRLK GENKQVMEYR RRLGEIMCWL
TEAENAMQKR SAAELEEDLQ ELTDLTQEMD VQAEKLKWLN RTELEMLSDK SLSLHEREKI
SESLRTVNST WNKICREVPS TLKEHIQEPC SVSQTRIAAH PGVQKVVLVS SASDIPVQSP
RTSEISIPAD LDKTITELAD WLVLIDQMLK SNIVTVGDIE EINKTVSRMK ITKSDLEQRH
PQLDYVFTLA QNLKNKASSS DVRTAITEKL EKVKNQWDST QHGVELRQQQ LEDMIIDSIQ
WDDHKEETEE LMRKYEARLY ILQQARRDPL IKQISDNQIL LQELGPGDGI IMAFDNVLQK
LLEEYGSDDT RNVKETTEYL KTSWINLKQS ITDRQSALEA ELRAVQASRR DLENFLKWIQ
EAETTVNVLA DASQRENALQ DTLLARELTQ QMQDIQAEID AHNDIFKSID GNRQKMVKAL
GNSEEATMLQ HRLDDMNQRW NDLKAKSASI RAHLEASAEK WNRLLTSLEE LIKWLNIKDE
ELQNQMPIGG DVPALQLQYD HCKALRRELK EKEYSVLNAI DQARVFLADQ PIEAPEEPRR
DLQSKTELTP EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM
DDLDVDMKEA EAVRNGWKPV GDLLIDSLQD HIEKTMAFRE EIAPINLKVK TVNDLSSQLS
PLDLHPSLKM SRQLDDLNMR WKLLQVSVDD RLKQLQEAHR DFGPSSQHFL STSVQLPWQR
SISHNKVPYY INHQTQTTCW DHPKMTELFQ SLADLNNVRF SAYRTAIKIR RLQKALCLDL
LELNTTNEVF KQHKLNQNDQ LLSVPDVINC LTTTYDGLEQ MHKDLVNVPL CVDMCLNWLL
NVYDTGRTGK IRVQSLKIGL MSLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ
IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKDFID WMRLEPQSMV WLPVLHRVAA
AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS GRTAKGHKLH YPMVEYCIPT
TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG YLPVQTVLEG DNLETPSQSP QLFHDDTHSR
IEQYATRLAQ MERTNGSFVT DSSSTTGSVE DEHALIQQYC QTLGGESPVS QPQSPAQILK
SVEREERGEL ERIIADLEEE QRNLQVEYEQ LKEQHLRRGL PVGSPPDSVV SPHHTSEDSE
LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPESDSRIN GVSPWASPQQ
SALSYSLDPD PDPQFHQAVA EDLLAPPHDT STDLTEFMEQ INSTFPSCCR NVKYSSSQPT
FPDIQYCPLQ QMPIPSSI
//
