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Database: UniProt
Entry: A0A1L8F450_XENLA
LinkDB: A0A1L8F450_XENLA
Original site: A0A1L8F450_XENLA 
ID   A0A1L8F450_XENLA        Unreviewed;      1939 AA.
AC   A0A1L8F450;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Myosin-4 {ECO:0000313|RefSeq:XP_018088868.1};
GN   Name=myh13.S {ECO:0000313|RefSeq:XP_018088868.1,
GN   ECO:0000313|Xenbase:XB-GENE-11536245};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018088868.1};
RN   [1] {ECO:0000313|RefSeq:XP_018088868.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018088868.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018088868.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   RefSeq; XP_018088868.1; XM_018233379.2.
DR   STRING; 8355.A0A1L8F450; -.
DR   PaxDb; 8355-A0A1L8F450; -.
DR   GeneID; 108700301; -.
DR   KEGG; xla:108700301; -.
DR   AGR; Xenbase:XB-GENE-11536245; -.
DR   CTD; 108700301; -.
DR   Xenbase; XB-GENE-11536245; myh13.S.
DR   OMA; RDAIYVI; -.
DR   OrthoDB; 2877572at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 108700301; Expressed in brain and 2 other cell types or tissues.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF77; MYOSIN-4 ISOFORM X1; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   REGION          660..682
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1153..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1278..1339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1912..1939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1168..1187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1939 AA;  223238 MW;  6FD44B74BE917A8D CRC64;
     MASDAEMSVF GLAAPFLRKP EKERLEAQNK PFDAKNSCFV HDDKELYVKG TIASRDSSKV
     TVNTVDDKTV TVKEEQVFPQ NPPKFDKIED MAMLTHLNEA SVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV AGYRGKKRQE APPHIFSISD NAYQFMLQDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA AIGDPGKKKE SINKLQGTLE DQIIQANPLL EAFGNAKTVR
     NDNSSRFGKF IRIQFGTTGK LSSADIETYL LEKSRVTFQL SAERSYHIFY QILTNKKPEI
     VEMLLLTTNP YDYSFISQGE ISVKSIDDEE ELMATDSAID ILGFNHDEKM GIYKMTGAVM
     HKGNMKFKQK QREEQAEPDG TEVADKIGYL MGLNSADLLK ALCYPRVKVG NEFVTKGQTV
     QQVYNSIGAL SKSVYEKLFL WMVTRINQQL DTKLPRQYFI GVLDIAGFEI FDLNSLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGID WEFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYDQHL GKCKNFEKPK PAKGKAEAHF SLVHYAGTVD YNICGWLEKN
     KDPLNETVVG LFQKSPVKLL SFLYSSYAGT DAAAEGGGKS GKKKKGSSFQ TVSALFRENL
     NKLMTNLRST HPHFVRCLIP NETKTPGIME NHLIIHQLRC NGVLEGIRIC RKGFPSRILY
     ADFKQRYKIL NANAIPEGQF IDSKKAAEKL LASIDVDHTQ YRFGHTKVFF KAGLLGVLEE
     MRDDKLAEII TKTQALCRGF LMRVEFKKMV ERRDAIYVIQ YNIRAFMNVK HWPWMKLYFK
     IKPLLKSAET EKEMANIKVE FDKTKEALAK SEARKKELEE KMVALLQEKN DLQLQCQSEF
     ENLADSEERC EGLIKNKINL EAKIKELTER LEDEEESNAE LTAKKRKLED ECSELKKDID
     DLELTLAKVE KEKHATENKV KNLTEEMSAL DDNISKIAKE KKALQEAHQQ TLDDLQAEED
     KVNSLSKAKT KLEQQVDDLE GSLEQEKKLR LDLERAKRKL EGDLKLAQET IMDLENDKQQ
     TDEKLKKKDF EMSQLQSRIE DEQTLASQLQ KKIKELQARI EEVEEEIEAE RAARAKVEKQ
     RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKVR RDLEESTLQH EATAAALRKK
     HADSVAELGE QLDNLQRVKQ KLEKEKSELK MEIDDLASNL ENVSKSKANI EKVSRMLEDQ
     LSEIKSKDDE HQRIINDLTG QKARLQTENG EQSRQLEEKE SLISQLSRGK QAFTQQTEEL
     KRQLEEESKA KNALAHALQS SRHDCDLLRE QYEEEQEAKA ELQRSLSKAN SEVAQWRTKY
     ETDAIQRTEE LEEAKKKLAQ RLQEAEEQVE AVNSKCASLE KTKQRLQGEV EDLMVDVERA
     NSVAAALDKK QRNFDKVLVE WKQKYEEGQS ELEAAQKEAR LLSTEIFKMK NAYEEALEHL
     ETMKRENKNL QQEISDLTEQ MGETVKNIHE LEKAKKQVEQ ERGDLQAALE EAEGSLEHEE
     AKILRIQLEL NQVKSEVDRK IAEKDEEIEQ LKRNTQRVID TMQSTLDSEI RSRNDALRLK
     KKMEGDLNEM EIQLGHANRQ ATEAQKQLRN VQAQLKDTQL QLDDAIRAQD DMKEQLAVVE
     RRTNLQQAEI EEMRSVLEQT ERSRKVAEQE LLDASERVQL LHSQNTSLLN TKKKLESDMV
     QLQGEVEETV QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN LEQTVKDLQH
     RLDEAEQLAM KGGKKQLQKL EARVRELENE LDAEQKRGSD GIKGVRKYER RVKELTYQTE
     EDRKNVLRLQ DLVDKLQLKV KAYKRQAEES EEQANAYMSR FRKVQHELEE AEERADIAES
     QVNKLRAKSR DIGKKGENE
//
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