ID A0A401PKB7_SCYTO Unreviewed; 3358 AA.
AC A0A401PKB7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Utrophin {ECO:0008006|Google:ProtNLM};
GN ORFNames=scyTo_0002646 {ECO:0000313|EMBL:GCB73566.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB73566.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB73566.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
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:GCB73566.1}.
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DR EMBL; BFAA01000676; GCB73566.1; -; Genomic_DNA.
DR STRING; 75743.A0A401PKB7; -.
DR OMA; DWCSTLM; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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; cd21234; CH_UTRN_rpt2; 1.
DR CDD; cd00176; SPEC; 7.
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; 6.10.140.70; -; 2.
DR Gene3D; 1.10.418.10; Calponin-like domain; 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; 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; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 9.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 5.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 16.
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; 1.
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:UP000288216};
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 33..137
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 152..257
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2831..2865
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 2989..3045
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 279..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..476
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 999..1026
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2343..2370
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2447..2524
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2698..2732
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3177..3214
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3248..3278
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 285..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3358 AA; 385543 MW; 80633A60473BA834 CRC64;
MAKVASGARN TVSSSPANEF GDIIRWRSDE HDGVQKKTFT KWINARFAKG GKIPIKDLFT
DLRDGRKLLD LLEGLTGNVL TKERGISRVH ALNNVTRALH VLQQNNVELV NIGGTDIVDG
NHKLTLGLIW SIILHWQVKD IMKAIMSDLQ QTNSEKILLS WVRQSTRPYK QVNVLNFTTS
WVDGLAFNAI VHRHKPGLFS WDKVLKMSAV GRLEHAFNMA KKHLGIEKLL DPEDVAVSLP
DKKSIIMYVT SLFEVLPQQV TMEDILEVET LPRQYKVEHA EGPLSRQKSV TSGKESLSSQ
TETSSTVPEM NVDLDSYQAV LEEVLTWLLS AEDTLHMQGD ISSDVEEVKE QFHIHEGFMM
ELTAHQSNVG NVLQAGNQLI AQGNLTDEEE NEIREQMALL NSRWESLRVA SMDRQAKLHE
VLMDLQQQQL QQLSDWLTRT EERIQKLEAQ STGDELESLK QQIDEHKLLQ SDLETEQVKV
NSLTHMVVVV DENSGESATA ALEDQLQSLG ERWAAVCRWT EERWRQLQDV FVKWQRLSED
QLLLDAWLTA KEDALTEVRT SSFKDQSESG VNIRRLAILK EDLEKKRPTL DHLGELGQAL
MKLLNNSNSS KKINSNTEEL SQRWNNLVQQ LEDYSKRVSR AFSELGITHV RPMEVVEMTT
EHSVQQQELV PPPPPKKRQL HMDVESKKKF DADARELLNW TDKSKCEIQA MMFNDFRKQK
DISGMKEKMK LEKIVKSKED WLKYTTSAAL KESCQYEINK LSEIVPCVEK LMARGEVFHK
EPGAPNFLHE DLSNFNHRFR SLLQKLQNKQ QVQAGLEGSQ SLDAVKSLKV LLDQSEAQVR
SNWSAIMNLE DAQNALKRTV KDADAVEKWM DRAETFLCKE TATLGNREGF QWQVEQCTTF
MNEIQNIQTN LTSMNEIQES LKMQPMSAIS KSMASHMVDY RTRWESLSNQ IKSQQTRLSE
GQEKTLNLRK DLAEMHKWTM LAEEEYLEKD FEYKSPEELE TSLEEMKRAK EEVLQKEVRV
KILKDNINTV LKKVSSSDQE IMSRDLHAVL ENYKRLCDRV ERKYLTLKEV WSCWCELLHY
LEIENNWLKN LDEMLYTTEN VPDSPEAVSE ALECLESVLR HPADNRTQIR ELGQTLIDGG
ILDELISEKL EVFNTRYEEL SHQAVSKQIS LEQHLQMSQE NEQRMHDLQE SLGLLDKQLT
LYLTDRIDAL QMPQEAQRKL REVSTKFQLF QKPANFEQRM LDCKSVLDGV KAELHVLDMR
SVEPEEIQPQ MDNCMKLYKT LSEVKLEVET VIKTGRQIVQ KQQTDNPKMM DEQLTALKLL
YNDMGAQVTE GKQDLEKALQ LSRKWKSETN SLSEWLTATE DKVIQRSSAR GIPVNLDSEI
KWSRLILKEL EVRKTELSSI TESSAALQGL IEGSERVLEN NLCTLNAIWN RVRTLTQGWC
DRLLDYQNQM EGFDQNVAHI STWLYQTEIL LDEINKKSDN EREEILQRFQ TELDGISLQV
DDVRDQAISL MNNNGTMCRE VVEPKLIELN RNVGRVSQHI KSAKMEATIK EPAKRDNGFR
PRLKTDQVSS IDLDRFEAEL QIKIDDLERK LQCSEEIPDD DEKVDEEEAD VEEMLQKGER
LLHLTNDDGK RKEIRKRLIL LQTKHASVKE AKLTQKEQVG ELSPGWYQYK KEENQFLQWL
DDIERQLLGY SGSGDEKKLQ ELIHVFEQRR EDFNVLTKKD QVLGGYSASP GKDSISVGKR
WRQIEIQLYT YQSLHLKSPD AQVITGYYTT SAGIAPQYFP SDYLLDINKT LLALADVELA
LNTPELNNGK YEDFSSQEDS LKNIKDMLEK LGEQIEDIHE NQPDALLEAS AAEVVQIGDT
LTQLHAEWDR VNRMYNDRKS CFDKAVEEWR RFHCDLNDLN QWVMEAEQIL PGARCQNGRL
DLEKARIHQQ ELEEGVSSHR PVYVTLNASG ADIIPELSSA DGCLLQEKLS GLNKRWRALS
VEVKDRHQRL EGDSQRYSDL RNQLDEFGLW LDKTQSALWA VHLPPREHDL KELKVPATDL
ESHSDNLTML NSIAQDVLSD KNLSLQERDI LSAKLRNINS NWSKVCKELP VKVKEIEIQL
QDYTHFKENL EKLSTWAIVA RQNLHPSGSP LPGTTQLQLL EAAMMDHRTG VETTLAKAVE
LDRKSHLLPE EKSKVAQLSV DWKTLNTALK DLSQQSVMGT SQSMSQPKVK VHSTVQTVTL
VSTTPPSGAT HLVLRDAFPP DSESLMPADL NKSALELIDW LTLIDQMIKS NIITVGDLEE
INKTIVRLKT TKNDLEQRQP QLDAIFTLAQ NLKNKTADLA ERAAVTERLV RVQNQWDNTQ
HRLEARQQQL EELLSDSIQW EEELQATERL VGQSEIHLQS MLQVTSDPLA PQLAESKHFL
QELHKGQFTV AAFNDLSSKL LRDYAADDTR KVKEVTDGIN TSWNNINQRA SERVGYLESE
LKQLQNLLQE LEGCLRWLQE AESAVDVLAK TAEKEDISLD SAEVKELKHR LHDIQAEIDA
HNDIFKSIDG NRHKMVKVLG NSEEAALLQY RLDDMNQRWS DLKTKSGNIR AHLEANAERW
TRLLASLEEL SKWLNLKDET LAKQMPIGGD VQTLLQQHDH CRALRHELME KEQTIITALD
SARLFLADQP IEGPEEPRRH LHVKTEPTPE ERAQRIAKAV RKQSTEVKEN WEQLNTNTSN
WQEQVEKALE KLQELQKAMD DLEAHVITAE GVRTDWQPVG DLLIDSLQDH IDKTTAFKEE
IAPVKEEVKI VNDLASQLSP LDVSLSPKTS HQLDDLSMRW KLIQVAVEDR IKQLQEAYRD
FGPSSQHFLS TSVQLPWQRA VSHNNKVPYY INHQTQSTCW DHPKMVELFH SLGDLNNVRF
SAYRTAMKIR RLQKALCYLF KQVAESTDSC DQRSLSLLLH DAVQIPRQLG EIASFGGSNI
EPSVRSCFQH GQNKSEIDAE QFVEWMRLEP QSMVWLPVLH RVAAAETAKH QAKCNICKEC
PIVGFRYRSL KHFNYDICQS CFFSGRTAKG HKLHYPMVEY CTPTTSGEDV RDFTKVLKNK
FRSKKYFAKH PRLGYLPVQT VLEGENLEIP VTLISMWPEQ YDPTQSPQLS QDDTHSRIEH
YANRLAQMER TNGSLLTDSS STTGSVEDEH ILIQQYCLTL GRESPISQPQ SPVQILKSVE
KEERSELEFI IANLEEEQRN LQAEYERLKQ QQILRDIKPL PSPTLSSNQQ NYHDAELLAE
AKLLRQHKGR LEARMQILED HNKQLESQLC RLRKLLEEPL TESKLNGVTA VSTTASFQLA
ENGQTCNEDF SSQTDDLLIP PQDTNTDLTD VMEQINSSFP VCSRKYTSGC ALYCALDL
//
