ID A0A452GZI0_9SAUR Unreviewed; 479 AA.
AC A0A452GZI0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Kelch-like protein 3 {ECO:0000256|ARBA:ARBA00023889};
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:ENSGAGP00000007473.1, 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:ENSGAGP00000007473.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the KLHL3 family.
CC {ECO:0000256|ARBA:ARBA00035639}.
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DR AlphaFoldDB; A0A452GZI0; -.
DR STRING; 38772.ENSGAGP00000007473; -.
DR Ensembl; ENSGAGT00000008629.1; ENSGAGP00000007473.1; ENSGAGG00000005975.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd18513; BACK_KLHL3; 1.
DR CDD; cd18339; BTB_POZ_KLHL3; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030578; KLHL3_BACK.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR PANTHER; PTHR24412:SF179; KELCH-LIKE PROTEIN 3; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 3.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 74..141
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 53853 MW; 05994EF6BC9051B0 CRC64;
MSCITSLWLE QLFQSYASKS FTPPLSPAFI KQSSQSPDEA EDKEKDQRTV TVNPSHMGKA
FKVMNELRSK RLLCDVVIVA EAIEMEAHRV VLAACSPYFC AMFTGDMTER KAKKIEIKDV
DGQTLSKLID YIYTAEIEVT EENVQVLLPA ASLLQLMDVR QNCCDFLQSQ LHPTNCLGIR
AFADVHTCTE LLQQANAYAE QHFPEVMLGE EFLNLSLDQV CSLISSDKLT VSSEEKVFEA
VISWINYEKE SRLEHMAELM EHVRLPLLPR DYLVQTVEEE ALIKNNNTCK DFLIEAMKYH
LLPLDQRQLI KNPRTKPRTP VSLPKVMIVV GGQAPKAIRS VECYDFEEDR WEQVAELPSR
RCRAGVVFMA GNIYAVGGFN GSLRVRTVDV YDGVKDQWTS IASMQERRST LGAAVLNELL
YAVGGFDGST GLASVEAYSY KTNEWFFVAP MNTRRSSVGV GVVEGKNNSS HFSHLNTAI
//
