MFA1A_MOUSE
ID MFA1A_MOUSE Reviewed; 439 AA.
AC C0HKD8; Q3TU29; Q8CCL1; Q9CQU1; Q9CSJ5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Microfibrillar-associated protein 1A {ECO:0000312|MGI:MGI:1914782};
DE AltName: Full=Spliceosome B complex protein MFAP1A {ECO:0000305};
GN Name=Mfap1a {ECO:0000312|MGI:MGI:1914782};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB28412.3}, and
RC NOD {ECO:0000312|EMBL:BAC40557.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB28412.3},
RC Embryonic liver {ECO:0000312|EMBL:BAB29385.1},
RC Head {ECO:0000312|EMBL:BAE36142.1},
RC Olfactory bulb {ECO:0000312|EMBL:BAC27936.1},
RC Pancreatic islet {ECO:0000312|EMBL:BAC34325.1}, and
RC Thymus {ECO:0000312|EMBL:BAC40557.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116 AND
RP SER-132, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-132
RP AND THR-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome. {ECO:0000250|UniProtKB:P55081}.
CC -!- SUBUNIT: Component of the spliceosome B complex. Interacts with PRPF38A
CC (via N-terminal interaction domain). {ECO:0000250|UniProtKB:P55081}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55081}.
CC -!- SIMILARITY: Belongs to the MFAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27936.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK012688; BAB28412.3; -; mRNA.
DR EMBL; AK014483; BAB29385.1; -; mRNA.
DR EMBL; AK032586; BAC27936.1; ALT_TERM; mRNA.
DR EMBL; AK050561; BAC34325.1; -; mRNA.
DR EMBL; AK077604; BAC36894.1; -; mRNA.
DR EMBL; AK088766; BAC40557.1; -; mRNA.
DR EMBL; AK161000; BAE36142.1; -; mRNA.
DR CCDS; CCDS16648.1; -.
DR RefSeq; NP_001075444.1; NM_001081975.3.
DR RefSeq; NP_080496.1; NM_026220.4.
DR AlphaFoldDB; C0HKD8; -.
DR SMR; C0HKD8; -.
DR STRING; 10090.ENSMUSP00000049548; -.
DR iPTMnet; C0HKD8; -.
DR PhosphoSitePlus; C0HKD8; -.
DR jPOST; C0HKD8; -.
DR PRIDE; C0HKD8; -.
DR DNASU; 67532; -.
DR Ensembl; ENSMUST00000056732; ENSMUSP00000049548; ENSMUSG00000048222.
DR Ensembl; ENSMUST00000089926; ENSMUSP00000087372; ENSMUSG00000068479.
DR GeneID; 100034361; -.
DR GeneID; 67532; -.
DR KEGG; mmu:100034361; -.
DR KEGG; mmu:67532; -.
DR CTD; 100034361; -.
DR CTD; 67532; -.
DR MGI; MGI:1914782; Mfap1a.
DR VEuPathDB; HostDB:ENSMUSG00000048222; -.
DR VEuPathDB; HostDB:ENSMUSG00000068479; -.
DR eggNOG; KOG1425; Eukaryota.
DR OMA; FHNERAG; -.
DR OrthoDB; 1535406at2759; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 100034361; 13 hits in 33 CRISPR screens.
DR BioGRID-ORCS; 67532; 9 hits in 31 CRISPR screens.
DR ChiTaRS; Mfap1a; mouse.
DR PRO; PR:C0HKD8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; C0HKD8; protein.
DR Bgee; ENSMUSG00000048222; Expressed in animal zygote and 76 other tissues.
DR ExpressionAtlas; C0HKD8; baseline and differential.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0001527; C:microfibril; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR InterPro; IPR033194; MFAP1.
DR InterPro; IPR009730; MFAP1_C.
DR PANTHER; PTHR15327; PTHR15327; 1.
DR Pfam; PF06991; MFAP1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CHAIN 2..439
FT /note="Microfibrillar-associated protein 1A"
FT /id="PRO_0000096459"
FT REGION 1..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55081"
SQ SEQUENCE 439 AA; 51954 MW; 5B57B1F1C42421E8 CRC64;
MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF
QFIKKAKEQE AEPEEQEEDS SSDPRLRRLQ NRISEDVEER LARHRKIVEP EVVGESDSEV
EGDAWRLERE DSSEEEEEEI DDEEIERRRG MMRQRAQERK NEEMEVMEVE DEGRSGEESE
SESEYEEYTD SEDEMEPRLK PVFIRKKDRV TVQEREAEAL KQKELEQEAK RMAEERRKYT
LKIVEEETKK ELEENKRSLA ALDALNTDDE NDEEEYEAWK VRELKRIKRE REDREALEKE
KAEIERMRNL TEEERRAELR ANGKVITNKA VKGKYKFLQK YYHRGAFFMD EDEEVYKRDF
SAPTLEDHFN KTILPKVMQV KNFGRSGRTK YTHLVDQDTT SFDSAWGQES AQNTKFFKQK
AAGVRDVFER PSAKKRKTT
