MFAP1_CAEEL
ID MFAP1_CAEEL Reviewed; 466 AA.
AC Q93712;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Microfibrillar-associated protein 1 {ECO:0000303|PubMed:22829783};
GN Name=mfap-1 {ECO:0000303|PubMed:22829783};
GN ORFNames=F43G9.10 {ECO:0000312|WormBase:F43G9.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 426-ASP-THR-427 AND ASP-426.
RX PubMed=22829783; DOI=10.1371/journal.pgen.1002827;
RA Ma L., Gao X., Luo J., Huang L., Teng Y., Horvitz H.R.;
RT "The Caenorhabditis elegans gene mfap-1 encodes a nuclear protein that
RT affects alternative splicing.";
RL PLoS Genet. 8:E1002827-E1002827(2012).
CC -!- FUNCTION: Involved in pre-mRNA splicing. {ECO:0000269|PubMed:22829783}.
CC -!- SUBUNIT: May be a component of the spliceosome.
CC {ECO:0000305|PubMed:22829783}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22829783}.
CC -!- TISSUE SPECIFICITY: Detected in intestine, pharynx, vulval muscles and
CC body wall muscles. {ECO:0000269|PubMed:22829783}.
CC -!- DISRUPTION PHENOTYPE: Developmental arrest at larval stage L1 or L2.
CC RNAi-mediated knockdown results in aberrant splicing of tos-1 mRNA with
CC increased intron 1 retention and exon 3 skipping, leading to increased
CC expression levels of tos-1 isoforms 1 and 2. However there is no
CC obvious recognition of the cryptic 3' splice site in tos-1 intron 1.
CC {ECO:0000269|PubMed:22829783}.
CC -!- SIMILARITY: Belongs to the MFAP1 family. {ECO:0000305}.
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DR EMBL; BX284601; CAB02103.1; -; Genomic_DNA.
DR PIR; T22141; T22141.
DR RefSeq; NP_492340.1; NM_059939.5.
DR AlphaFoldDB; Q93712; -.
DR SMR; Q93712; -.
DR STRING; 6239.F43G9.10; -.
DR EPD; Q93712; -.
DR PaxDb; Q93712; -.
DR PeptideAtlas; Q93712; -.
DR EnsemblMetazoa; F43G9.10.1; F43G9.10.1; WBGene00009671.
DR GeneID; 172661; -.
DR KEGG; cel:CELE_F43G9.10; -.
DR UCSC; F43G9.10; c. elegans.
DR CTD; 172661; -.
DR WormBase; F43G9.10; CE10372; WBGene00009671; mfap-1.
DR eggNOG; KOG1425; Eukaryota.
DR HOGENOM; CLU_023077_1_0_1; -.
DR InParanoid; Q93712; -.
DR OMA; FHNERAG; -.
DR OrthoDB; 1535406at2759; -.
DR PhylomeDB; Q93712; -.
DR PRO; PR:Q93712; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009671; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:WormBase.
DR InterPro; IPR033194; MFAP1.
DR InterPro; IPR009730; MFAP1_C.
DR PANTHER; PTHR15327; PTHR15327; 2.
DR Pfam; PF06991; MFAP1; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..466
FT /note="Microfibrillar-associated protein 1"
FT /id="PRO_0000438775"
FT REGION 1..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 426..427
FT /note="DT->VA: In n4564 n5214; temperature sensitive
FT phenotype with embryonic lethality at 25 degrees Celsius
FT and wild type phenotype at 15 degrees Celsius. Splicing of
FT tos-1 mRNA is defective with increased intron 1 retention
FT and exon 3 skipping, although there is no obvious
FT recognition of the cryptic 3' splice site in tos-1 intron
FT 1."
FT /evidence="ECO:0000269|PubMed:22829783"
FT MUTAGEN 426
FT /note="D->V: In n5214; no effect on tos-1 mRNA splicing."
FT /evidence="ECO:0000269|PubMed:22829783"
SQ SEQUENCE 466 AA; 55945 MW; 4281C6A7BC01D520 CRC64;
MGDYVPGFEQ RESDNRSFGH SRLPTLGAIP IKNEKGQTVM QKVKVSRYVA GKAPEYARNY
DSDSSESDRE TDRDDDRRRR RRRESSDEED RRRHRRHEDY GRRRQVEKPE VLGKVEDESS
ENEQESEEDE EKQEERRERA RMRRLELHEN NREKDEEQED SAESDEEDFE RRRQMLRDRA
IKREEEIKRE IKEELEEDDV EEEEEEESSE EEDSDEDDDP VPRLKPIFTR KKDRITLQEA
EKEKEKEILK KIEDEKRAEE RKRESAKLVE KVLQEEEAAE KRKTEDRVDL SSVLTDDETE
NMAYEAWKLR EMKRLKRNRD EREEAAREKA ELDKIHAMSE EERLKYLRLN PKVITNKQDK
GKYKFLQKYF HRGAFFLDEE DEVLKRNFAE ATNDDQFDKT ILPKVMQVKN FGKASRTKYT
HLTEEDTTDH QGVWASTNQL NSQFSTKRAG GSRPVFERPA TKKRKN
