ID A0A2Y9QNR9_TRIMA Unreviewed; 3440 AA.
AC A0A2Y9QNR9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Utrophin isoform X3 {ECO:0000313|RefSeq:XP_023585125.1};
GN Name=LOC101358359 {ECO:0000313|RefSeq:XP_023585125.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023585125.1};
RN [1] {ECO:0000313|RefSeq:XP_023585125.1}
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_023585125.1; XM_023729357.1.
DR Proteomes; UP000248480; 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; 9.
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; 18.
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:UP000248480};
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 36..140
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 155..260
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2818..2851
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3071..3127
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 289..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3282..3304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3349..3379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 454..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 775..818
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 884..911
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1104..1193
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1695..1755
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2692..2719
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 289..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3440 AA; 395188 MW; B6BB08899C73930D CRC64;
MSCPVTTTFR WKTYRFDLPG QVALQACRRL PDEHNDVQKK TFTKWINARF SKSGKPPISD
MFTDLKDGRK LLDLLEGLTG TSLPKERGST RVHALNNVNR VLQVLHQNNV DLVNIGGTDI
VDGNHKLTLG LLWSIILHWQ VKDVMKDIMS DLQQTNSEKI LLSWVRQSTR PYGQVNVLNF
TTSWTDGLAF NAVLHRHKPD LFSWDRVVKM SPTQRLEHAF SKAQTYLGIE KLLDPEDVAV
QLPDKKSIIM YLTSLFEVLP QQVTIDDIRE VETLPRKYKK ECEEGEINIQ STVPEEERES
PRAETPSTVT EVDVDLDSYQ IALEEVLTWL LSAEDTFQEQ DDISDNVEEV KDQFAIHEAF
MMELTAHQSS VGSVLQAGNQ LITQGTLTDE EEFEIQEQMT LLNARWEALR VESMERQSRL
HDVLMELQKR QLQQLSAWLT LTEERIQKME ACPLDDDLQS IQKLLEEHKS LQNDLETEQV
KVNSLTHMVV IVDENSGENA TAILEDQLQK LGERWTAVCR WTEERWNRLR EINILWQELL
EEQCLLKAWL TEKEEALNKV QTSNFKDQKE LSVSIRRLAI LKEDMEMKRQ ALDQLSEIGQ
DVGQLLDNTK ASKKINSDSE ELTQRWDSLV QRLEDSSNQV TQVVAKLGMS QIPQKDLLET
VRIREQVTTK KSKQELPPPP PPKKRQIHVD IEAKKKFDAV SAELLNWILK SKTAIQTTEM
KEYKKMQETS ELKKKLKELE KEQAERSPKL DELSQTGQIL LEQMRKGGLP AEEIKNTLEK
VLSEWKRQSQ HLEDLARKIQ LQEEINSYFK QLDELEKTIK KKEEWVKHTP FSEPPQQSLP
SLKDSCQREL TNLLGLHPKI EMLLASCLAL KSQLSAPDFV QKSLDSFLGR YQALQRDLED
RQQQLENELK SQPGREYLET MKTLKDTLND SENKAQASLS VLNDLAKVEK TLQEKKALDE
ILESQKPTLY KLAEETKALE KNAPPDVENT YRQEFDAVEG KWNKLKAKVS KDLYLLEEIT
PKLRTFETDS EAIAKWMDGV KDFLKKERAA QGDADGLQRQ LDQCSAFVNE IEAVESSLKD
MKEIEANLRS CPVAGIKTWV QTKLSEYQTQ LEKFSKEIAI QKNRLSESQE KAVNLKKDLA
EMQEWMAQAE EEYLERDFEY KSPEELESAV EEMKRAKEDV LQKEVRVKIL KDNIKLLATK
VPSGGQELTS ELNVVLENYQ LLCNRIRGKC HTLEEVWSCW IELLHYLDLE TSWLNALEER
MKSTEVLPEK AEAVSEALES LESVLRHPAD NRTQIRELGQ TLIDGGILDD IISEKLEAFN
SRYEELSHLA ENKQISLEKQ LQVLRETDHM LQVLQESLAE LDKQLTTYLT DRIDAFQVPQ
EAQKIQAEIS AHELTLEELR RNMRPQPSTS PDGRTTRGGS QMDVLQRKLR EVSTKFQLFQ
KPANFEQRML DCKRVLDGVK AELHVLDVKD VDPDVIQTHL DKCMKLYKTL SEVKLEVETV
IKTGRHIVQK QQTDNPKGMD EQLTSLKVLY NDLGAQVTEG KQDLERASQL ARKMKKESAS
LSDWLSVTEA ELVQKSTSEG LLCDLDTEIS WAKNVLKDLE KKKADLNTIT ESSAALQNLI
EGSETILEEK LCVLNAGWSR VRTWTEDWCN TLMNHQNQLE IFDGNVAHIS TWLYQAEALL
DEIEKKPASK REEIVKRLIS EVDDANLQVE NVRDQAIILM NARGGSSREL VEPKLAELNR
NFEKVSQHIK SAKLLIDQEP LSYQYLVGTE AFEAGPPSSD LDRLESDIQN MLNIVEKHLE
SSDGDEKLDE ERAQIEEVLQ RGEQMLHQPM EDSTKEKIRL QLILLRTRYN KVKAIPTQQR
KTAQLASRVR SLPLPTDYLV EINKVLHTMD DIELSLNTPE LNTAVYEDFS FQEDSLKNIK
DQLDKLGEQI AVIHEKQPDV MLEASGPEAV QIGDALTQLN AKWDGVNRIY NDCKGYSDRA
LEEWRQFNCD LNDLTQWITE VKQLLVDTCA PDGSLDLEKA RIHQQELEEG ISSHQPSFAA
LNGTGDSIVQ KLSSTSGSFL KDKLAGLNQR WSAVTAEVKA RQPRLKEERK QVMEYRKRLD
EIICWITKAE NAVQKTSTTE LEENLRELTD LTQEMEVQAD KLKWLNRTEL EMLSDKSLSL
QEREKISESL RTVNTTWNKV YRELPIALKE RIQEPSPVSP TRTAAPPSVQ KVVLVSSTPD
IPVQSHRTSE ISIPADLDKT ITELADWLVL IDQMLKSNIV TVGDIEEINK TVSRMKITKA
DLEQRRPQLD YVFTLAQNLK NKASSSDVRT AITEKLEKVQ SQWDSTQHGV QSRQQQLEDM
IMDSLQWDDH REEMEELMRK YEAQLYILQQ ARRDPLIKQI SDNQILLQEL GLGDGIVMAF
DNVLQKLLEE YGNDDTRNVK ETTEYLKSSW INLKQSIADR QSALEAELRT VQASRRDLEN
FLKWIQEGET TVNVLEDASQ RENALQDSTM ARELKQQMQD IQAEIDAHND IFKSIDGNRQ
KMVKALGNSE EATMLQHRLD DMNQRWNDLK AKSASIRAHL EASAEKWNRL LTSLEELIKW
LNMKDEELKK QMPIGGDVPA LQLQYDHCKA LRRELKEKEY SVLNAIDQAR VFLADQPIEA
PEEPRRNLQT KTELTPEERA QKIAKAMRKQ SSEVKEKWES LNAVTSNWQK QVDKALEKLR
DLQGAMDDLD ADMKEVEAVR NGWKPVGDLL IDSLQDHIEK TMAFREEIAP INLKVKTVND
LSSQLSPLDL HPSLKMSRQL DDLNMRWKLL QVAVDDRLKQ LQEAHRDFGP SSQHFLSTSV
QLPWQRSISH NKVPYYINHQ TQTTCWDHPK MTELFQSLAD LNNVRFSAYR TAIKIRRLQK
ALCLDLLELN TTNEVFKQHK LNQNDQLLSV PDVINCLTTT YDGLEQIHKD LVNVPLCVDM
CLNWLLNVYD TGRTGKIRVQ SLKIGLISLS KGLLEEKYRY LFKEVAGPTE MCDQRQLGLL
LHDAIQIPRQ LGEVAAFGGS NIEPSVRSCF QQNNNKPEIS VKEFIDWMRL EPQSMVWLPV
LHRVAAAETA KHQAKCNICK ECPIVGFRYR SLKHFNYDVC QSCFFSGRTA KGHKLHYPMV
EYCIPTTSGE DVRDFTKVLK NKFRSKKYFA KHPRLGYLPV QTVLEGDNLE TPSQSPQLFH
DDTHSRIEQY ATRLAQMERT NGSFLTDSSS TTGSVEDEHA LIQQYCQTLG GESPMSQPQS
PAQILKSVER EERGELERII ADLEEEQRNL QVEYEQLKEQ HLKRGLPVSS PPDSVVSPHH
TSEDSELIAE AKLLRQHKGR LEARMQILED HNKQLESQLH RLRQLLEQPE SDPRINGVSP
WASPQHSALS YSLDPDPGPQ FQQAAAEDLL APPHETSTDL TEVMEQINST FPSCCTNLPS
RPQVRLNELT DSNVADHNLD
//
