MKLN1_PONAB
ID MKLN1_PONAB Reviewed; 735 AA.
AC Q5RB35;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Muskelin;
GN Name=MKLN1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex
CC that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1 (By similarity). Required for internalization
CC of the GABA receptor GABRA1 from the cell membrane via endosomes and
CC subsequent GABRA1 degradation. Acts as a mediator of cell spreading and
CC cytoskeletal responses to the extracellular matrix component THBS1 (By
CC similarity). {ECO:0000250|UniProtKB:O89050,
CC ECO:0000250|UniProtKB:Q9UL63}.
CC -!- SUBUNIT: Homodimer; may form higher oligomers (By similarity).
CC Identified in the CTLH complex that contains GID4, RANBP9 and/or
CC RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B),
CC GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or
CC alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or
CC RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5
CC have ancillary roles (By similarity). Interacts with RANBP9 (By
CC similarity). Part of a complex consisting of RANBP9, MKLN1 and GID8 (By
CC similarity). Interacts with GABRA1 (By similarity). Interacts with the
CC C-terminal tail of PTGER3 (By similarity).
CC {ECO:0000250|UniProtKB:O89050, ECO:0000250|UniProtKB:Q99PV3,
CC ECO:0000250|UniProtKB:Q9UL63}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O89050}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:O89050}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O89050}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:O89050}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:O89050}. Synapse {ECO:0000250|UniProtKB:O89050}.
CC Postsynapse {ECO:0000250|UniProtKB:O89050}. Note=Colocalizes with
CC GABRA1 at synapses and in postsynaptic regions. Colocalizes with actin
CC fibers in the cell cortex. {ECO:0000250|UniProtKB:O89050}.
CC -!- DOMAIN: The LisH mediates head to tail dimerization.
CC {ECO:0000250|UniProtKB:Q99PV3}.
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DR EMBL; CR858822; CAH91025.1; -; mRNA.
DR RefSeq; NP_001125592.1; NM_001132120.1.
DR AlphaFoldDB; Q5RB35; -.
DR SMR; Q5RB35; -.
DR STRING; 9601.ENSPPYP00000020207; -.
DR Ensembl; ENSPPYT00000049147; ENSPPYP00000025343; ENSPPYG00000018010.
DR GeneID; 100172508; -.
DR KEGG; pon:100172508; -.
DR CTD; 4289; -.
DR eggNOG; KOG2437; Eukaryota.
DR GeneTree; ENSGT00390000001702; -.
DR InParanoid; Q5RB35; -.
DR OrthoDB; 145268at2759; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0002090; P:regulation of receptor internalization; ISS:UniProtKB.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR010565; Muskelin_N.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF06588; Muskelin_N; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Cytoplasm; Kelch repeat; Nucleus;
KW Reference proteome; Repeat; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UL63"
FT CHAIN 2..735
FT /note="Muskelin"
FT /id="PRO_0000286398"
FT DOMAIN 172..204
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 206..258
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 284..330
FT /note="Kelch 1"
FT REPEAT 339..391
FT /note="Kelch 2"
FT REPEAT 408..458
FT /note="Kelch 3"
FT REPEAT 469..515
FT /note="Kelch 4"
FT REPEAT 526..578
FT /note="Kelch 5"
FT REPEAT 597..651
FT /note="Kelch 6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL63"
SQ SEQUENCE 735 AA; 84800 MW; 1B241C551DF8092C CRC64;
MAAGGAVAAA PECRLLPYAL HKWSSFSSTY LPENILVDKP NDQSSRWSSE SNYPPQYLIL
KLERPAIVQN ITFGKYEKTH VCNLKKFKVF GGMNEENMTE LLSSGLKNDY NKETFTLKHK
IDEQMFPCRF IKIVPLLSWG PSFNFSIWYV ELSGIDDPDI VQPCLNWYSK YREQEAIRLC
LKHFRQHNYT EAFESLQKKT KIALEHPMLT DIHDKLVLKG DFDACEELIE KAVNDGLFNQ
YISQQEYKPR WSQIIPKSTK GDGEDNRPGM RGGHQMVIDV QTETVYLFGG WDGTQDLADF
WAYSVKENQW TCISRDTEKE NGPSARSCHK MCIDIQRRQI YTLGRYLDSS VRNSKSLKSD
FYRYDIDTNT WMLLSEDTAA DGGPKLVFDH QMCMDSEKHM IYTFGGRILT CNGSVDDSRA
SEPQFSGLFA FNCQCQTWKL LREDSCNAGP EDIQSRIGHC MLFHSKNRCL YVFGGQRSKT
YLNDFFSYDV DSDHVDIISD GTKKDSGMVP MTGFTQRATI DPELNEIHVL SGLSKDKEKR
EENVRNSFWI YDIVRNSWSC VYKNDQAAKD NPTKSLQEEE PCPRFAHQLV YDELHKVHYL
FGGNPGKSCS PKMRLDDFWS LKLCRPSKDY LLRHCKYLIR KHRFEEKAQM DPLSALKYLQ
NDLYITVDHS DPEETKEFQL LASALFKSGS DFTALGFSDV DHTYAQRTQL FDTLVNFFPD
SMTPPKGNLV DLITL
