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Database: UniProt
Entry: H2ZSQ0_LATCH
LinkDB: H2ZSQ0_LATCH
Original site: H2ZSQ0_LATCH 
ID   H2ZSQ0_LATCH            Unreviewed;      1171 AA.
AC   H2ZSQ0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Atrophin 1 {ECO:0000313|Ensembl:ENSLACP00000000421.1};
GN   Name=ATN1 {ECO:0000313|Ensembl:ENSLACP00000000421.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000421.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000000421.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; AFYH01260002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01260003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01260004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01260005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2ZSQ0; -.
DR   STRING; 7897.ENSLACP00000000421; -.
DR   Ensembl; ENSLACT00000000423.1; ENSLACP00000000421.1; ENSLACG00000000377.1.
DR   eggNOG; KOG2133; Eukaryota.
DR   GeneTree; ENSGT00940000153615; -.
DR   HOGENOM; CLU_005292_0_0_1; -.
DR   InParanoid; H2ZSQ0; -.
DR   OMA; YPHSLES; -.
DR   TreeFam; TF328554; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000000377; Expressed in muscle tissue and 6 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   InterPro; IPR017993; Atrophin-1.
DR   InterPro; IPR002951; Atrophin-like.
DR   PANTHER; PTHR13859:SF9; ATROPHIN-1; 1.
DR   PANTHER; PTHR13859; ATROPHIN-RELATED; 1.
DR   Pfam; PF03154; Atrophin-1; 2.
DR   PRINTS; PR01222; ATROPHIN.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..196
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..335
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..817
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1171 AA;  125548 MW;  D8112061A09F0BC7 CRC64;
     MKTRQNKDSM SMRSGRKKES TSPNEELRLR GRASPGDGSS SSSDSKAEKP RPSSKVDLGQ
     VERYICLSII VSEPRQGAEV CLSIIVSKPK PGANKISPQG ISRPGSPSDI ESLDGRSVND
     DTSSDPRDID QDNRSTSPSI PSPGSPESDS DSSVSQDPKP YTPLLPTQMS SPPPAPPPPP
     PPQALLNPPQ IPSSDPEQDP EPLEDFTNTD PPKQPQPQIE TQASRIFQST QAQAPVQSSS
     IFPPSQPFPA QPLASQSNMR MMTPNLSSQP RDQSLPVRHP PPTNPLPVNT GLSFQKLTAY
     PATTFPHVSS NLPPPPALKP LNTPSGHPHP SPAHNAPLPI MQQSAANHPP PSTAPQVVEK
     APGQSHPLLP SSGPVSNPAR YPYAPASCQT SSSQSVVSYT SSYSHPFPPS TNSVNSQPPK
     YTQPSLSSQP VWSQTLPYSR SFPPHSSFNQ SSHSQASGSS HYSSGHHIYP PHSSHPGSSQ
     AGAFPLPPES SNPSVTQSSH IYPPSSHPSG HSAIRSYSQN SSHLGQSQSY VSSNLPASQP
     PPPPSQAHPT TNQLPSYPYS GSHPAAVHPT HGSVPITTSA PAPVASVIST VTSSIANIPP
     SFKTASPPAA SLGAAPAYKM APSPGSTIPM VPTFKTMSPP TATIPSASAY RAASSPGITP
     PFKAGSPAAA SIPLAPMPAS APVPVAAVSG VPPQAPPLPA IIQIKEEPVD ESEEPESPMP
     SNLSPSPEPK VVDIASHASQ SARFIKHLDR GYNSCARTDF YFVPLEGSKL AKKRADVLER
     ARREAEQKVR EEKERERERE REKEREKELE RAAKIPPDSR APESISIGAA GPRPPFEPQG
     GTVATVPPYL GPDTPALRTL SEYARPHVMS PTNRNHPFYV PLGSADPLLG YNVPAIYSSD
     PGARERELRE REARERELRE RELRERLKPG FEVKPSELEA LHPVANPMDP FTRHGGIALQ
     AAPGLNPFTP FHPGLSPLER ERLALAAGPV LRPDMSYAER LAAERQHAER LAALGNDPLA
     RLQMLNVTPH HHQHSHIHSH LHLHQQDAIH AAAASVHPLI DPLASGSPLT RIPFSGASIP
     NSLLAHPIHE NEVLRHQLFG APFRDLPAAL PAPMSAAHQL QAMHAQSTEL QRLALEQHQQ
     WLHAHHPLHG VPLPGQDDYY SHLKKESDKP L
//
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