ID K7GFK5_PELSI Unreviewed; 3443 AA.
AC K7GFK5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Utrophin {ECO:0000313|Ensembl:ENSPSIP00000019066.1};
GN Name=UTRN {ECO:0000313|Ensembl:ENSPSIP00000019066.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000019066.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000019066.1}
RP IDENTIFICATION.
RG Ensembl;
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: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR002341}.
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DR EMBL; AGCU01203629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01203638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 13735.ENSPSIP00000019066; -.
DR Ensembl; ENSPSIT00000019154.1; ENSPSIP00000019066.1; ENSPSIG00000016602.1.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000153467; -.
DR HOGENOM; CLU_000246_2_0_1; -.
DR OMA; DWCSTLM; -.
DR TreeFam; TF320178; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0070938; C:contractile ring; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Ensembl.
DR GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0017166; F:vinculin binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
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; -; 12.
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; 8.
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; 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:UP000007267};
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 2819..2852
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3072..3128
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 3363..3385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 887..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1164..1191
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1335..1407
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1686..1713
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1799..1826
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2601..2628
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2686..2720
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3260..3294
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 3364..3385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3443 AA; 395617 MW; FB7C56FF977613CB CRC64;
MATVSDQEEG PGGGHNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPIKDMFTEL
KDGRKLLDLL EGLTGNPLPK ERGSTRVHAL NNVNRVLQVL HQNNVELVNI GGTDIVDGNH
KLTLGLLWSI ILHWQVKDVM KDIMSDLQQT NSEKILLSWV RQSTRPYSQV NVLNFTTSWT
DGLAFNAVIH RHKPELFSWD KVTKSSPTER LEHAFTIAKN ELGIDKLLDP EDVAVQLPDK
KSIIMYLTSL FEVLPQQVTM EDIREVETLP RRYKKECEEG VFNIQQSATS EEEQGGSRAE
TPSTVTEVNM DLDSYQEALE EVLMWLLTAE DTYQEQDEIS EDVEKVKEQF STHEFFMMEL
TKHQSNVGSV LQAGNQLISQ GNLTEEEELE IQEQMTLLNA RWESLRVDSM DRQSRLHDVL
MELQKKQLQQ LSDWLTVTEE RIQKMESPAL VEDLESLQKQ MEVHKGLQHD LEIEQVKVNS
LTHMVVIVDE NSGESATAVL EDQLQRLGER WTAVCHWTEE RWMKLQDIQM LWQELVEEQC
LLKAWLTDKE DALNKIQIRN FKDQTELSAN VRKLAILKED MGIKRQMLDE LSELGQDVAL
LVGNNRTSKK IDSDLEELTQ KWDSLVQKLE EFSNQVTWAV ENTGVSQVSQ NTESEMFSAK
EQIMVKQSKQ EVTPPPPPKK RQIPVDIEAK KRFDAENAEL LNWILKSKAA IQAIEIKEYK
KMRETSNLKE KLKTLEKETI EKSPKLDGLS QSGQNMLDQM GKEGPFTEDV KNAMEKILTE
WKEVIGHLEG LARNIQYQDE INAYVSEMGE LEKIVNEKEL WLKNAGTLAL QQQPLIALKE
SCQRELTHLL SLCPQIEQQT AACKVLASQP AAPSFIQDSL SGFTDHFRSV QQKLEEQHEQ
LKKAKTELEC QPSQDYLDTL KRLKEILNEL ESKDQSIMTA MSDQSQVERA LQQRKTICET
LEDQKPTIDK LAAETKALEK HASFDIAKIY KQEFKNIQGQ WDKLKLQFTK DVHLLEEIVS
QLRIFEADSK IIQKWMDGVK DFLMKEQAIQ GDSEGLQRQL DQCTTLVNEM EKTELSLKEM
KEVESTLRLQ PIGVDTWVKS RLVDFQAQWE KLSKQIVTQK NRLSESQEKT VNLKKDLAEM
QEWMTQAEEE YLERDFEYKS PEELENAVEE MKRAKEDVLQ KEVRVKILKD NIKVLAAKVP
SGGQHLTSEL NIVLENYQLL CNRIRGKCHT LEEVWSCWIE LLQYLDLETA WLNALEERVQ
STENLPDKLN AVNEALESLE SVLRHPADNR TQIRELGQTL IDGGILDDII SEKLEAFNAR
YEELSHLAVS RQIALEQQLR TMRETEHMLQ VLQENLAELD RQLNSYLTDR IDAFQMPQEA
QKIQAEIAVH ESTLEELKKN ARSLSSASSE CRSPRGGTPL DALQRKLREV STKYQLFQKP
ANFEQRMLDC KRILDSVKAE LHVLDVKDTD PDVIQGHLDK CMKLYKTLSE VKLEVETVIK
TGRQIVQKQQ TDNPKGMDEQ LTALKFLYND LGAQVTEGKQ DLERALQLAC KMKKETASLS
EWLATTETEL VQKSTSESLL ADLDTEIAWA KNVLRELERR KVDLDTITES SAALQTLVEG
SENSLEEKLC VLNAGWSRVR TWTEDWCNTL LNHQNQLEIF DENVAHISTW LYQAEALLDE
TEKKPASKKE KTVKRLTSEL DDVSLRVDNV RDQAVILMNS RGVPCRELVE PKLSELNRNF
DKVSQHIKSA KILIGQEPLP YKVPVEPELQ EPAVASADLD KFESDLQNML KVVEKHMASS
DEDEKMDEER AQIEEVLQRG ERLLQQPMED NKREKIRLQL LLLQTRHNNV KPIPALRLKS
KYPSGSRTSP FPTEYLVEIN RVLLAMADVE LLLNAPELNT HVYEDFSTQE DSLKNIKDIL
DRLGDQIAVI HEKQPDVILE ASGPESIQIG DALTQLNAEW DRINRMYNDK KCCFDRAVED
WRQFHCDLND LTQWITEADG LLADARAPDG SLDLETAGLH QQELEEGVSS HQTSFSTLNR
TGEGIIQKLS TTDGSFLQEK LAGLNKRWKA IIAEIMDRQQ RLKGENQQLM DYRKKLDEFS
CWLENVENSL EMRPTFNHEQ HLQELKGLTV EMEIQGEKLQ WLNRTEVEVL SDKKIGFQER
ERISDTLRTV NVKWNKLFQE VPERVRELEA YVQQLYPVTQ SKLSAHPAVQ NVVLLSSSFE
APVQTQQVLE LSAPADLDKT TTELADWLVL IDQMLKSNIV TVGNVEEINR TIARMKITKE
DLEQRHPQLD SVFTLAQNLK NKTSSSDVRT VITEKLEKVK NQWDNTQHGV EVRQQQLKYM
LSDSIHWDEQ RKEMEQLIEQ NEIRLHTLLQ APKQTLIKQI SENKLLIQEL LKGDITVAAF
NDLSNKLLRD YCDDDTRKVK EITDHLNISW INLNQRTGDR QNALEVELKI VQTLLRDLEG
FVKWMQEAET TVNVLADASQ RENALEDSAC TGELKKQIQD IQAEIDAHND IFKSIDGNRH
KMVKALGNSE EAALLQHRLD DMNQRWNDLK AKSASIRAHL EANADKWNKL LTSLEELIKW
LNVKDEELKK QMPIGGDVPT LQQQYDRCKA LRRELKDKEQ TILNAVDQAR VFLADQPIEG
PEEPRKNLHS KMVWLTPEEK AQRIAKAMRK QSSEVKEKWD SLNASANSWQ KQVDKALEKL
KDVQCAMDDL DADLKEAENV RNGWKPVGDL LIDSLQEHVE KTTAFREEIA PINLKVKTLN
DLSSQLSPLD LHPSLKMSRQ LDDLNMRWKL LQVSVEDRLK LLQEAHQDFG PTSQHFLSTS
VQLPWQRSVS HNKVPYYINH QTQTTCWDHP KMSELFQSLA DLNNVRFSAY RTAIKIRRLQ
KALCLDLLDL NTTNEVFKQH KLSQNDQLLS VQDVISCLTT AYSGLEEKHK DMVNVPLCVD
MCLNWLLNVY DTGRTGKIRV QSLKIGLMSL SKGLLEEKYR YLFKEVAGHT EMCDQRQLGL
LLHDAIQIPR QLGEVAAFGG SNIEPSVRSC FQQNHNKPEI TVKQFIDWMH LEPQSMVWLP
VLHRVAAAET AKHQAKCNIC KECPIVGFRY RSLKHFNYDV CQSCFFSGRT AKGHKLHYPM
VEYCIPTTSG EDVRDFTKVL KNKFRSKKYF AKHPRLGYLP VQTVLEGDNL EAPITLISMW
PEQYDPSQSP QLFHDDTHSR IEQYATRLAQ MERNNGSLLT DSSSTTGSVE DEHALIQQYC
QTLGGESPVS QPQSPAQILK SVEKEERGEL ERIIADLEEE QRSLQVEYEQ LKEQHLRRGI
NPLASPPDSA VSPQHMSEDA ELIAEAKLLR QHKGRLEARM QILEDHNKQL ESQLHRLRQL
LEQPESDSRV NGVSPCSSPQ YSAHSYSLDQ DASSQFYQPV SCADDLLVPP HDTNTDLTDV
MEQINSTFPT CCLPLPPSMP SAM
//
