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Database: UniProt
Entry: A0A452HQ37_9SAUR
LinkDB: A0A452HQ37_9SAUR
Original site: A0A452HQ37_9SAUR 
ID   A0A452HQ37_9SAUR        Unreviewed;       693 AA.
AC   A0A452HQ37;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000017131.1};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000017131.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000017131.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   AlphaFoldDB; A0A452HQ37; -.
DR   Ensembl; ENSGAGT00000019552.1; ENSGAGP00000017131.1; ENSGAGG00000010121.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   CDD; cd09327; LIM1_abLIM; 1.
DR   CDD; cd09328; LIM2_abLIM; 1.
DR   CDD; cd09329; LIM3_abLIM; 1.
DR   CDD; cd09330; LIM4_abLIM; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR   Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR   InterPro; IPR032402; AbLIM_anchor.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR036886; Villin_headpiece_dom_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24213; ACTIN-BINDING LIM PROTEIN; 1.
DR   PANTHER; PTHR24213:SF18; ACTIN-BINDING LIM PROTEIN 1; 1.
DR   Pfam; PF16182; AbLIM_anchor; 2.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 6.
DR   SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..693
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019578590"
FT   DOMAIN          68..127
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          128..187
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          195..254
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          625..693
FT                   /note="HP"
FT                   /evidence="ECO:0000259|PROSITE:PS51089"
FT   REGION          310..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  78689 MW;  8692989C97FC3B32 CRC64;
     MLGLGFLLRF SLPSFFFLPC LFVLCLHAHL VCEGRKILYS FSYSNVLYFI FTVAHSQEPP
     HSTEKPVIHC HKCEEPCKGE VLRVQSKHFH IKCFTCKVCG CDLAQGGFFI KNGEYLCSVD
     YQRMYGTRCN GCGEFVEGEV VTALGKTYHP NCFACTVCKR PFPPGDRVTF NGRDCLCQMC
     AQPMSSSPKE ISSSSNCAGC GREIKNGQAL LALDKQWHLG CFKCKACGKV LTGEYISKDG
     APYCEKDYQV LFGVKCEACH QFITGKVLEA GDKHYHPSCA RCSRCNQMFT EGEEMYLQGS
     TVWHPDCKQS TKAEDKLRPT RTSSESIYSR PGSSIPGSPG HTIYAKVDNE ILDYKDLAAI
     PKVKAIYDIE RPDLITYEPF YTSAYEERQE RQSLGESPRT LSPTPSAEGY QDVRDRMIHR
     STSQGSISSP VYSRHSYTPT MSRSPQHFHR PGNEPSSGRN SPVPYRPDSR PLTPTYVQAP
     KHFHVPDQGI NIYRKPPIYK QHGVDMRRRS SGREEEDEEL QRRRQLQEEQ LMKLNSGLGQ
     LILKEEMEKE TRDRPPLLAS RYDSPINSSS QASASKTSSL PGYGRNGLHR VRWQQCGEAE
     GGVNSLPDGH VPGMRMDRGV SMPNMLEPKI FPYEMLMVTN RGRNKILRDV DRTRLERHLA
     PEVFQEIFGM TIQEFDKLPL WRRNDMKKKA KLF
//
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