HNRPM_RAT
ID HNRPM_RAT Reviewed; 690 AA.
AC Q62826; Q5M815;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein M;
DE Short=hnRNP M;
DE AltName: Full=M4 protein;
GN Name=Hnrnpm; Synonyms=Hnrpm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA83442.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:AAA83442.2};
RX PubMed=11406629; DOI=10.1074/jbc.m104093200;
RA Bajenova O.V., Zimmer R., Stolper E., Salisbury-Rowswell J., Nanji A.,
RA Thomas P.;
RT "Heterogeneous RNA-binding protein M4 is a receptor for carcinoembryonic
RT antigen in Kupffer cells.";
RL J. Biol. Chem. 276:31067-31073(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 55-68; 182-196; 245-260 AND 612-625.
RC TISSUE=Liver {ECO:0000269|PubMed:10947964};
RX PubMed=10947964; DOI=10.1042/bj3500495;
RA Kafasla P., Patrinou-Georgoula M., Guialis A.;
RT "The 72/74-kDa polypeptides of the 70-110 S large heterogeneous nuclear
RT ribonucleoprotein complex (LH-nRNP) represent a discrete subset of the
RT hnRNP M protein family.";
RL Biochem. J. 350:495-503(2000).
RN [4]
RP PROTEIN SEQUENCE OF 60-68 AND 418-423, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535; SER-548 AND SER-661, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Pre-mRNA binding protein, binds avidly to poly(G) and poly(U)
CC RNA homopolymers. Involved in splicing. Acts as a receptor for
CC carcinoembryonic antigen in Kupffer cells, may initiate a series of
CC signaling events leading to tyrosine phosphorylation of proteins and
CC induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha
CC cytokines. {ECO:0000269|PubMed:11406629}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC Interacts with PPIA/CYPA (By similarity).
CC {ECO:0000250|UniProtKB:P52272}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16128803}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11406629};
CC IsoId=Q62826-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62826-2; Sequence=VSP_051766;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including liver,
CC heart, lung, skeletal muscle, kidney, stomach, large intestine, small
CC intestine, pancreas, spleen, peritoneal macrophage and thyroid.
CC {ECO:0000269|PubMed:11406629}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83442.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U32577; AAA83442.2; ALT_INIT; mRNA.
DR EMBL; BC088317; AAH88317.1; -; mRNA.
DR RefSeq; NP_001103381.1; NM_001109911.1.
DR RefSeq; NP_446328.2; NM_053876.2.
DR AlphaFoldDB; Q62826; -.
DR SMR; Q62826; -.
DR BioGRID; 250540; 5.
DR IntAct; Q62826; 3.
DR MINT; Q62826; -.
DR STRING; 10116.ENSRNOP00000032108; -.
DR CarbonylDB; Q62826; -.
DR iPTMnet; Q62826; -.
DR PhosphoSitePlus; Q62826; -.
DR jPOST; Q62826; -.
DR PeptideAtlas; Q62826; -.
DR PRIDE; Q62826; -.
DR GeneID; 116655; -.
DR KEGG; rno:116655; -.
DR UCSC; RGD:620369; rat. [Q62826-1]
DR CTD; 4670; -.
DR RGD; 620369; Hnrnpm.
DR eggNOG; KOG4212; Eukaryota.
DR InParanoid; Q62826; -.
DR OrthoDB; 1174365at2759; -.
DR PhylomeDB; Q62826; -.
DR Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q62826; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042382; C:paraspeckles; ISO:RGD.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990405; F:protein antigen binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; TAS:RGD.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:1990831; P:cellular response to carcinoembryonic antigen; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:1904591; P:positive regulation of protein import; IDA:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR CDD; cd12661; RRM3_hnRNPM; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR024667; HnRNP_M.
DR InterPro; IPR024666; HnRNP_M_PY-NLS.
DR InterPro; IPR034990; hnRNPM_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23003:SF6; PTHR23003:SF6; 5.
DR Pfam; PF11532; HnRNP_M_NLS; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CHAIN 2..690
FT /note="Heterogeneous nuclear ribonucleoprotein M"
FT /id="PRO_0000081866"
FT DOMAIN 70..148
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 164..241
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 360..365
FT /note="1"
FT REPEAT 367..372
FT /note="2"
FT REPEAT 375..380
FT /note="3"
FT REPEAT 386..391
FT /note="4"
FT REPEAT 393..398
FT /note="5"
FT REPEAT 400..405
FT /note="6"
FT REPEAT 406..411
FT /note="7"
FT REPEAT 413..418
FT /note="8"
FT REPEAT 421..426
FT /note="9"
FT REPEAT 428..433
FT /note="10"
FT REPEAT 435..440
FT /note="11"
FT REPEAT 442..447
FT /note="12"
FT REPEAT 453..458
FT /note="13"
FT REPEAT 460..465
FT /note="14"
FT REPEAT 467..472
FT /note="15"
FT REPEAT 474..479
FT /note="16"
FT REPEAT 481..486
FT /note="17"
FT REPEAT 488..493
FT /note="18"
FT REPEAT 500..505
FT /note="19"
FT REPEAT 507..512
FT /note="20"
FT REPEAT 514..519
FT /note="21"
FT REPEAT 522..527
FT /note="22"
FT REPEAT 528..532
FT /note="23"
FT REPEAT 535..540
FT /note="24"
FT REPEAT 541..545
FT /note="25"
FT REPEAT 548..553
FT /note="26"
FT REPEAT 563..568
FT /note="27"
FT DOMAIN 613..689
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..568
FT /note="27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-
FT [MLVI]-[GAV]"
FT COMPBIAS 40..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D0E1"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 456
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 625
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 632
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0E1"
FT MOD_RES 658
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 341
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 627
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52272"
FT VAR_SEQ 1..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051766"
FT CONFLICT 55
FT /note="R -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="S -> G (in Ref. 2; AAH88317)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="T -> A (in Ref. 2; AAH88317)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="I -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 73782 MW; 4FF9B6D6BD9B1F43 CRC64;
MAAGVEAAAE VAATEPKMEE ESGAPCVPSG NGAPVPKGEE RPTQNEKRKE KNIKRGGNRF
EPYANPTKRY RAFITNIPFD VKWQSLKDLV KEKVGEVTYV ELLMDAEGKS RGCAVVEFKM
EESMKKAAEV LNKHSLSGRP LKVKEDPDGE HARRAMQKAG RLGSTVFVAN LDYKVGWKKL
KEVFSMAGVV VRADILEDKD GKSRGIGTVT FEQSIEAVQA ISMFNGQLLF DRPMHVKMDE
RALPKGDFFP PERPQQLPHG LGGIGMGLGP GGQPIDANHL NKGIGMGNLG PAGMGMEGIG
FGINKIGGME GPFGGGMENM GRFGSGMNMG RINEILSNAL KRGEIIAKQG GSGAGGSVPG
IERMGPGIDR ISGAGMERMG AGLGHGMDRV GSEIERMGLV MDRMGSVERM GSGIERMGPL
GLDHMASSIE RMGQTMERIG SGVERMGAGM GFGLERMAAP IDRVGQTIER MGSGVERMGP
AIERMGLSMD RMVPTGMGAG LERMGPVMDR MATGLERMGA NNLERMGLER MGANSLERMG
LERMGANSLE RMGPAMGPAL GAGIERMGLA MGGAGGASFD RTIEMERGNF GGSFAGSFGG
AGGHAPGVAR KACQIFVRNL PFDFTWKMLK DKFNECGHVL YADIKMENGK SKGCGVVKFE
SPEVAERACR MMNGMKLSGR EIDVRIDRNA
