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Database: UniProt
Entry: A0A3B1J7A0_ASTMX
LinkDB: A0A3B1J7A0_ASTMX
Original site: A0A3B1J7A0_ASTMX 
ID   A0A3B1J7A0_ASTMX        Unreviewed;      1925 AA.
AC   A0A3B1J7A0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized LOC103024598 {ECO:0000313|Ensembl:ENSAMXP00000038108.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000038108.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000038108.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|RuleBase:RU000487}.
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DR   Ensembl; ENSAMXT00000042122.1; ENSAMXP00000038108.1; ENSAMXG00000040643.1.
DR   GeneTree; ENSGT00940000166728; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000040643; Expressed in embryo and 13 other cell types or tissues.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF390; ACTIN-LIKE ISOFORM X1; 1.
DR   Pfam; PF00022; Actin; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT   DOMAIN          31..153
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|Pfam:PF13716"
FT   REGION          522..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1100..1127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1203..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1434..1467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..977
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..993
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1317..1360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1925 AA;  214604 MW;  E48DB70D542B6624 CRC64;
     MSGSSAGTFD QHGCPLVMFP TESQDKLVSD LTKEEVADFI SYFLRLHSKN KEECLVSVVA
     DLREANLSIA RRVAESLLLL ELHRRTVHSV YVVQPRKRDA LKLLQKLLLP KKASYSPQNA
     YKCVFLKEVC ELWNYIDRSQ LTASLGGYLV YCHSSWVSFV KEIDSFVQQF VAVVQRLPVC
     ISALQSISAL PVPADPSRLS QFCSSNQAEL QQIRSDLGLD ELLRRCECVL EKFRFPESDQ
     CYQAMVGTHL YTHTALEMLH NYERITAAVE KVELLWQQAF SKARGQLQLL NLQKEAQQVE
     SQMDLVWQKL QSFSTETAAD GGSAETLKLE FEASVYTHAM ALVRRAEDVI HTLVENVGER
     SVGEQWVVEL EQQKERFRSA VELQYSNIRT HCLFHQLHNK IQSWYSLAVC ESFLQDLLWV
     TCCTEQDSQG DVSAGREWRP ALESFLRVHT CPQVEELVQL AHLANVISDP QLQNAGKQLA
     HRCMNLRKLL TSPGSATLRD LQLALQWQYE YLKGSRETVN SDLIPRRNES TETVDSERSV
     QRDSGFVSIM ASVRPSSSHP DLNKQDCVKN NPLRSAVLPD AASLAGKPPS LSSFDSGFEG
     AGGGQIEGKE GQDGLPRMPY SRETTSRLKV PQLQISEENV SSMSDSEDLD HGTAGSNSTT
     ASIHIIPRIT SDSLNFEIKV QRSATLPKNP WLSLPVDNLE SSYTVTISPS SPALQRPPKC
     HSPSEHCRDQ PTQTDSQGCG YSTKQQDHEG SFREGEFSPI RNVLSSTMAE GGDQADGTTD
     VPHTLLWDTY DLHDVRQDTS DRLSDISLGN WELEEQKELQ AVEEILGRTA GILQEEENVL
     AQEVALDVLL KADHVGRQWP SWNHMSSSEL AEAGVIGLED DPTSPLRFNC RDSVSSSRPN
     SEAISPAEQL LQPDRSRVLQ ELEDLQVLEE RIMEENMKIQ ELRLSEKTPE SRRKFLEELE
     REKKEVEEME RSLRRETKKK REGKPKKRSQ RGPKVVKCSI MEMTMALQSF EDEDAVCDEA
     LLMNCRRETQ ESKSLQSNSR HLDTATDGFI SCLDSGQSCT AMSVGLATEE FGHSIDVDQF
     HEDYTKSVPS NSALDEIVHF PDKDQPHEPP DLITEDSTSS RPSNSGLREI INCESSNQPC
     ASANFSTTEE STNSSPSNLI IDKLIDCVDS DQLCEPQDLT TEDSSLSRPS DSPLDELINC
     AVSEQHRKTP DLTTEESTSF GPSDLSPSKI MECADSNQNH EQPLQLTTED SSLSRPLNPV
     LEEIIQDLNQ IVLDSHCKDA ELGTDPPLIA ITKKPTNNDL YLSVDQDEDK QSIHSSPSKT
     DGDVFTPGNS LITHTGSQMK ETGQQMDTSK SGMNENPSEI MKESWKTDES ESQSGDLKLM
     EACQERAAFD PGGPKPHPRL QRMKKPLMHS GESSVSELNL ETCDHHDEFV VTGSTLLPSA
     GPKPKERKNL PPRIYPSAAE HNRNNNNPRC ADLYRLDAET FLQEPAVEYV EYEAVDHTDV
     DIVSQISETE SHGVCNKSAA KVTNTRIDEE PSTRTVCTSP ALHQQLQICS REASEFLTPV
     VLDTGSGLVK AGFADQDLPS LIFPTAIGVP KYEEVMSSSV QQAVYVGHDA QHMRGVLTLH
     YPMKNGIIDN WDQIEMIWQH VFRQLGVDPE DHPVLLTEGV LNPQGNRQRM VQTMFETFNV
     PLTFIALQPV LALYAAGRTT GVVFDSGDGV SHSVPVFDGY SLPHAVQRLT LAGSDVTMQL
     KKLLLEQGVC MRTSAELEIV RDIKERCCCV ALDFEVQLSK GGGASTPTHY TLPDGQIVSL
     TTERFRAPEI LFKPELIGRD HYGIHESIFR SVLQSDIDLR KSFLGNIVLS GGNTLLAGLP
     ERLQVELGNL APATECVKVI SAPDRDFSVW KGGAVLSSLP TFSSAWISRD EYEEFGPNIV
     NRRCF
//
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