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Database: UniProt
Entry: A0A2U3VPK2_ODORO
LinkDB: A0A2U3VPK2_ODORO
Original site: A0A2U3VPK2_ODORO 
ID   A0A2U3VPK2_ODORO        Unreviewed;      3441 AA.
AC   A0A2U3VPK2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Utrophin isoform X1 {ECO:0000313|RefSeq:XP_004397096.1};
GN   Name=UTRN {ECO:0000313|RefSeq:XP_004397096.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004397096.1};
RN   [1] {ECO:0000313|RefSeq:XP_004397096.1}
RP   IDENTIFICATION.
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_004397096.1; XM_004397039.2.
DR   STRING; 9708.A0A2U3VPK2; -.
DR   GeneID; 101366169; -.
DR   KEGG; oro:101366169; -.
DR   CTD; 7402; -.
DR   InParanoid; A0A2U3VPK2; -.
DR   OrthoDB; 2880153at2759; -.
DR   Proteomes; UP000245340; 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; 11.
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; 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; 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:UP000245340};
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          2811..2844
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          3064..3120
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          661..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1392..1415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3356..3376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1098..1187
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2114..2141
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2685..2712
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3252..3286
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1395..1410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3441 AA;  395216 MW;  B4674131FCF5F22C CRC64;
     MAKYGEHEAR PDDGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFTDL
     KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVDLVNI GGTDIVDGNH
     KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT NSEKILLSWV RQSTRPYSQV NVLNFTTSWT
     DGLAFNAVLH QHKPDLFSWD RVVKMSPIER LEHAFGKAQT YLGIEKLLDP EDVAVQLPDK
     KSIIMYLTSL FEVLPQQVTL DAIREVETLP RKYKKECEEG EISLQSSVLE EEHESPGAET
     PSTVAEVDMD LDSYQIALEE VLTWLLSAED TFQEQEDIAD DVEEVKDQFA THEAFMMELT
     AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR WEALRVDSMD RQSRLHDVLM
     ELQKRQLEQL SAWLMLTEER IQKMETRPLD DDLKSLQKLL EDHKCLQNDL EAEQVKVNSL
     THMVVIVDEN SGESTTALLE DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL
     LKAWLTEKEE ALNKVQTSNF KDQKELSVSI RRLAILKEDM EMKRQALDQL SEIGQDVGQL
     LDNPKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK ALLETVRVRE
     QVTTKRSKQE LPPPPPKKRQ IPVDTEAKKK FDAVSAELLN YILKSKTAIQ ATEIKGYKKM
     QETSEMKKKL KGFEKEQTER SPRLDELNQT GQILLEQMGK EGIPMEEIKN VLEKVFSEWK
     DVSQRLEDLA RKIQLQEDIN AYFKQLDDLE KTIKAKEEWV KHTPFLESPQ QPLPSLKDSC
     QRELADLLSL HPRIERAHAG CSALRSRPSA PDFVRQAFES LLGRYQAVRQ DLEHHQQQLE
     NELKSQPGHA YLETLKTLKE TLNDSESKAQ TSLNALNDLP KVAKALQERK ALDEILENQK
     PTLYKLAEET KSLEKNVSPD VEKMYKQEFD DVQGKWNKLK VKVSKDLHLL EEITSRLKAF
     EADLKVIEKW MDGVKDFLMK EQVVQGDAEG LQSQLDQCSA FVNEIETVES SLKDMKEIEA
     NLRSCPVAGI KTWMQTKLVD YQTQSEKLSK EIAIQKNRLS ESQEKAVNLK KDLSEMQEWM
     TQAEEEYLER DFEYKSPEEL ESAVEEMKRA KEDVLQKEVR VKILKDNIML LAAKAPSGGQ
     ELTSELNVVL ENYQLLCNRI RGKCHTLEEV WSCWIELLHY LDLETCWLST LEERMKSTEA
     LPEKSDAVNE ALESLESVLR HPADNRTQIR ELGQTLIDGG ILDDIISEKL EAFNSRYEDL
     SHLAESKQIA LEKQLQVLRE TDHMLQVLQE SLGELDKQLT TYLTDRIDAF QVPQEAQKIQ
     AEISAHELTL EELRRNTRSQ PPTSPEGRNA RGGSQMDLLQ RKLREVSTKF QLFQKPANFE
     QRMLDCKRVL DCVKAELHVL DVKDVDPDVI QSHLDKCMKL YKTLSEVKLE VETVIKTGRH
     IVQKQQTDNP RGMDEQLTSL KILYNDLGAQ VTEGKQDLER ASQLARKMKK ETASLSEWLS
     VTEAELVQKS TSEGLLGDLD IEISWAKNIL KDLEKRKADL NTITESSAAL KNLIEGSEPV
     LEERLCVLNA GWSRVRTWTE DWCNTLMNHQ NQLEIFDGNV AHISTWLYQA EALLDEIEKK
     PASKREEIVK RLISELDDAN LQVENVRDQA IVLMNARGGS SRELVEPKLA ELNRNFEKVS
     QHIRSAKLLI GQEPLAYQCL VTTEAFEADV LFSDLEKLES GIENMLKVVE KHLEFSDEDE
     KMDEERAQIE EVLQRGEQML HQPMEDNKKE KIRLQLLLLR TRYNKTKAVP NQQTTGQLAP
     GTRSPPLPTD YLVEINKVLL SVDDAELSLN APELSTVVYE DFSFQEDSLK NIKDQLDKLG
     EQIAVIHEKQ PDVILEASGP EAIQIRDILT QLNGKWDRIN RMYNDRKGHF DRAMEEWRQF
     HCDLNDLTQW ITEAEELLAE TLAPDGSLDL EKAGMYQQEL EEGISSHQPS FAALNRTGDG
     IVQKLSPMDG SFLKDKLAGL NQRWSAIFAE VKDRRPRLKG ESKQVMDYRK RLDDIICWLT
     KAENALQKRS TTELEENLQE LTDLTQEMDV QAEKLKWLNR NELEMLSDKS LSLHEREKIS
     ESLRTVNSTW NKICREVPST LKERIQEPCS VSQTRIAAHP GVQKVVLVSS ASDIPAQSPR
     TSEISVPADL DKTITELADW LVLIDQMLKS NIVTVGDIEE INKTVSRMKI TKADLEQRHP
     QLDYVFTLAQ NLKNKASSSD VRTAITEKLE KVKNQWDSTQ HGVELRQQQL EDMIIDSLQW
     DDHREETEEL MRKYEARLYI LQQARRDPLI KQISDNQILL QELGPGDGIV MAFDNVLQKL
     LEDYGSDDTR NVKETTEYLK TSWINLKQSI ADRQSALEAE LRTVQASRRD LENFLKWIQE
     AETTVNVLAD ASQRENVLQD TVLARELTRQ LQDIQAEIDA HNDIFKSIDG NRQKMVKALG
     NSEEATMLQH RLDDMNQRWN DLKAKSASIR AHLEASAEKW NRLLTSLEEL IKWLNVKDEE
     LQKQMPIGGD VPALQLQYDH CKALRRELKE KEYSVLNAID QARVFLADQP IEAPEEPRRN
     LQSKTELTPE ERAQKIAKAM RKQSSEVKEK WESLNAVTSN WQKQVDKALE KLRDLQGSMD
     DLDVDMKEAE AVRNGWKPVG DLLIDSLQDH IEKTMAFREE IAPINLKVKT VNDLSSQLSP
     LDLHPSLKMS RQLDDLNMRW KLLQVSVDDR LKQLQEAHRD FGPSSQHFLS TSVQLPWQRS
     ISHNKVPYYI NHQTQTTCWD HPKMTELFQT LADLNNVRFS AYRTAIKIRR LQKALCLDLL
     ELNTTNEVFK QHKLNQNDQL LSVPDVINCL TTTYDGLEQM HKDLVNVPLC VDMCLNWLLN
     VYDTGRTGKI RVQSLKIGLM SLSKGLLEEK YRYLFKEVAG PTEMCDQRQL GLLLHDAIQI
     PRQLGEVAAF GGSNIEPSVR SCFQQNNNKP EISVKEFIDW MRLEPQSMVW LPVLHRVAAA
     ETAKHQAKCN ICKECPIVGF RYRSLKHFNY DVCQSCFFSG RTAKGHKLHY PMVEYCIPTT
     SGEDVRDFTK VLKNKFRSKK YFAKHPRLGY LPVQTVLEGD NLETPVTLIS MWPEHYDPSQ
     SPQLFHDDTH SRIEQYATRL AQMERTNGSF LTDSSSTTGS VEDEHALIQQ YCQTLGGESP
     VSQPQSPAQI LKSVEREERG ELERIIADLE EEQRSLQVEY EQLKEQHLRR GFPVGSPPDS
     VVSPHHTSED SELIAEAKLL RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ LLEQPESDSR
     INGVSPWASP QQSALSYSLD PDPGPQFHQA AAEDLLSPPH DTGTELTEFM EQITSTFPSC
     CPNLPSRPQV RVNGVDWLRD C
//
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