MKLN1_HUMAN
ID MKLN1_HUMAN Reviewed; 735 AA.
AC Q9UL63; A4D1M8; A6NG43; Q9NSK4; Q9NUS8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Muskelin;
GN Name=MKLN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, Lung, and Osteosarcoma;
RX PubMed=10640805; DOI=10.1159/000015385;
RA Adams J.C., Zhang L.;
RT "cDNA cloning of human muskelin and localisation of the muskelin (MKLN1)
RT gene to human chromosome 7q32 and mouse chromosome 6 B1/B2 by physical
RT mapping and FISH.";
RL Cytogenet. Cell Genet. 87:19-21(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 320-735.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP INTERACTION WITH RANBP9, AND IDENTIFICATION IN A COMPLEX WITH RANBP9 AND
RP GID8.
RX PubMed=12559565; DOI=10.1016/s0378-1119(02)01153-8;
RA Umeda M., Nishitani H., Nishimoto T.;
RT "A novel nuclear protein, Twa1, and Muskelin comprise a complex with
RT RanBPM.";
RL Gene 303:47-54(2003).
RN [9]
RP IDENTIFICATION IN THE CTLH COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=17467196; DOI=10.1016/j.gene.2007.02.032;
RA Kobayashi N., Yang J., Ueda A., Suzuki T., Tomaru K., Takeno M., Okuda K.,
RA Ishigatsubo Y.;
RT "RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins
RT ARMC8alpha and ARMC8beta are components of the CTLH complex.";
RL Gene 396:236-247(2007).
RN [10]
RP FUNCTION, AND INTERACTION WITH RANBP9.
RX PubMed=18710924; DOI=10.1083/jcb.200801133;
RA Valiyaveettil M., Bentley A.A., Gursahaney P., Hussien R., Chakravarti R.,
RA Kureishy N., Prag S., Adams J.C.;
RT "Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator
RT of cell morphology regulation.";
RL J. Cell Biol. 182:727-739(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
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 (PubMed:29911972). Required for
CC internalization of the GABA receptor GABRA1 from the cell membrane via
CC endosomes and subsequent GABRA1 degradation (By similarity). Acts as a
CC mediator of cell spreading and cytoskeletal responses to the
CC extracellular matrix component THBS1 (PubMed:18710924).
CC {ECO:0000250|UniProtKB:O89050, ECO:0000269|PubMed:18710924,
CC ECO:0000269|PubMed:29911972}.
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 (PubMed:17467196, PubMed:29911972). Within
CC this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC MKLN1, ARMC8 and YPEL5 have ancillary roles (PubMed:29911972).
CC Interacts with RANBP9 (PubMed:18710924). Part of a complex consisting
CC of RANBP9, MKLN1 and GID8 (PubMed:12559565). Interacts with GABRA1.
CC Interacts with the C-terminal tail of PTGER3 (By similarity).
CC {ECO:0000250|UniProtKB:Q99PV3, ECO:0000269|PubMed:12559565,
CC ECO:0000269|PubMed:17467196, ECO:0000269|PubMed:18710924,
CC ECO:0000269|PubMed:29911972}.
CC -!- INTERACTION:
CC Q9UL63; Q9BWK5: CYREN; NbExp=3; IntAct=EBI-1048053, EBI-8787584;
CC Q9UL63; Q9UL63: MKLN1; NbExp=3; IntAct=EBI-1048053, EBI-1048053;
CC Q9UL63; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-1048053, EBI-2515601;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17467196}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL63-2; Sequence=VSP_021852;
CC -!- DOMAIN: The LisH mediates head to tail dimerization.
CC {ECO:0000250|UniProtKB:Q99PV3}.
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DR EMBL; AF047489; AAF06698.1; -; mRNA.
DR EMBL; AK002024; BAA92042.1; -; mRNA.
DR EMBL; AC018642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24081.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83782.1; -; Genomic_DNA.
DR EMBL; BC002834; AAH02834.2; -; mRNA.
DR EMBL; BC067825; AAH67825.1; -; mRNA.
DR EMBL; AL162071; CAB82407.1; -; mRNA.
DR CCDS; CCDS34754.1; -. [Q9UL63-1]
DR PIR; T47173; T47173.
DR RefSeq; NP_001138826.1; NM_001145354.1.
DR RefSeq; NP_001308245.1; NM_001321316.1. [Q9UL63-2]
DR RefSeq; NP_037387.2; NM_013255.4. [Q9UL63-1]
DR AlphaFoldDB; Q9UL63; -.
DR SMR; Q9UL63; -.
DR BioGRID; 110435; 128.
DR CORUM; Q9UL63; -.
DR IntAct; Q9UL63; 50.
DR MINT; Q9UL63; -.
DR STRING; 9606.ENSP00000323527; -.
DR GlyGen; Q9UL63; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UL63; -.
DR PhosphoSitePlus; Q9UL63; -.
DR BioMuta; MKLN1; -.
DR DMDM; 23821862; -.
DR EPD; Q9UL63; -.
DR jPOST; Q9UL63; -.
DR MassIVE; Q9UL63; -.
DR MaxQB; Q9UL63; -.
DR PaxDb; Q9UL63; -.
DR PeptideAtlas; Q9UL63; -.
DR PRIDE; Q9UL63; -.
DR ProteomicsDB; 84959; -. [Q9UL63-1]
DR ProteomicsDB; 84960; -. [Q9UL63-2]
DR Antibodypedia; 18008; 154 antibodies from 22 providers.
DR DNASU; 4289; -.
DR Ensembl; ENST00000352689.11; ENSP00000323527.6; ENSG00000128585.18. [Q9UL63-1]
DR GeneID; 4289; -.
DR KEGG; hsa:4289; -.
DR MANE-Select; ENST00000352689.11; ENSP00000323527.6; NM_013255.5; NP_037387.2.
DR UCSC; uc011kpm.3; human. [Q9UL63-1]
DR CTD; 4289; -.
DR DisGeNET; 4289; -.
DR GeneCards; MKLN1; -.
DR HGNC; HGNC:7109; MKLN1.
DR HPA; ENSG00000128585; Low tissue specificity.
DR MIM; 605623; gene.
DR neXtProt; NX_Q9UL63; -.
DR OpenTargets; ENSG00000128585; -.
DR PharmGKB; PA30828; -.
DR VEuPathDB; HostDB:ENSG00000128585; -.
DR eggNOG; KOG2437; Eukaryota.
DR GeneTree; ENSGT00390000001702; -.
DR HOGENOM; CLU_004210_1_0_1; -.
DR InParanoid; Q9UL63; -.
DR OMA; DPISENV; -.
DR OrthoDB; 145268at2759; -.
DR PhylomeDB; Q9UL63; -.
DR TreeFam; TF323659; -.
DR PathwayCommons; Q9UL63; -.
DR SignaLink; Q9UL63; -.
DR BioGRID-ORCS; 4289; 37 hits in 1076 CRISPR screens.
DR ChiTaRS; MKLN1; human.
DR GeneWiki; MKLN1; -.
DR GenomeRNAi; 4289; -.
DR Pharos; Q9UL63; Tbio.
DR PRO; PR:Q9UL63; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UL63; protein.
DR Bgee; ENSG00000128585; Expressed in calcaneal tendon and 187 other tissues.
DR ExpressionAtlas; Q9UL63; baseline and differential.
DR Genevisible; Q9UL63; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 GO; GO:0007165; P:signal transduction; NAS:ProtInc.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Kelch repeat; Nucleus; Reference proteome; Repeat; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..735
FT /note="Muskelin"
FT /id="PRO_0000119138"
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021852"
FT VARIANT 469
FT /note="C -> G (in dbSNP:rs323844)"
FT /id="VAR_050057"
FT CONFLICT 6
FT /note="A -> M (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="N -> Y (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="I -> N (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="S -> G (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="Q -> K (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="G -> A (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="T -> N (in Ref. 1; AAF06698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 84768 MW; 1A8F06FE1DE9193D 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 KHRFEEKAQV DPLSALKYLQ
NDLYITVDHS DPEETKEFQL LASALFKSGS DFTALGFSDV DHTYAQRTQL FDTLVNFFPD
SMTPPKGNLV DLITL
