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FGF12_MOUSE
ID   FGF12_MOUSE             Reviewed;         243 AA.
AC   P61329; O35339; P70376; Q924B4; Q92912; Q93001;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Fibroblast growth factor 12;
DE            Short=FGF-12;
DE   AltName: Full=Fibroblast growth factor homologous factor 1;
DE            Short=FHF-1;
DE   AltName: Full=Myocyte-activating factor;
GN   Name=Fgf12; Synonyms=Fhf1;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=8790420; DOI=10.1073/pnas.93.18.9850;
RA   Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H.,
RA   Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.;
RT   "Fibroblast growth factor (FGF) homologous factors: new members of the FGF
RT   family implicated in nervous system development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9232594; DOI=10.1016/s0925-4773(97)00042-7;
RA   Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D., Goldfarb M.;
RT   "Murine FGF-12 and FGF-13: expression in embryonic nervous system,
RT   connective tissue and heart.";
RL   Mech. Dev. 64:31-39(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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 nervous system development and function. Promote
CC       neuronal excitability by elevating the voltage dependence of neuronal
CC       sodium channel SCN8A fast inactivation. {ECO:0000250|UniProtKB:P61328}.
CC   -!- SUBUNIT: Interacts with the C-terminal region of SCN9A. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P61329-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P61329-2; Sequence=VSP_010223;
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC       {ECO:0000305}.
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DR   EMBL; U66201; AAB18917.1; -; mRNA.
DR   EMBL; AF020738; AAB71607.1; -; mRNA.
DR   EMBL; AK034335; BAC28679.1; -; mRNA.
DR   EMBL; BC030485; AAH30485.1; -; mRNA.
DR   CCDS; CCDS28092.1; -. [P61329-1]
DR   CCDS; CCDS88909.1; -. [P61329-2]
DR   RefSeq; NP_001263348.1; NM_001276419.2.
DR   RefSeq; NP_034329.1; NM_010199.4. [P61329-2]
DR   RefSeq; NP_898887.1; NM_183064.5. [P61329-1]
DR   AlphaFoldDB; P61329; -.
DR   SMR; P61329; -.
DR   BioGRID; 199641; 10.
DR   STRING; 10090.ENSMUSP00000097601; -.
DR   iPTMnet; P61329; -.
DR   PhosphoSitePlus; P61329; -.
DR   SwissPalm; P61329; -.
DR   MaxQB; P61329; -.
DR   PaxDb; P61329; -.
DR   PeptideAtlas; P61329; -.
DR   PRIDE; P61329; -.
DR   ProteomicsDB; 267464; -. [P61329-1]
DR   ProteomicsDB; 267465; -. [P61329-2]
DR   ABCD; P61329; 1 sequenced antibody.
DR   Antibodypedia; 33876; 245 antibodies from 32 providers.
DR   DNASU; 14167; -.
DR   Ensembl; ENSMUST00000100024; ENSMUSP00000097601; ENSMUSG00000022523. [P61329-1]
DR   Ensembl; ENSMUST00000232352; ENSMUSP00000155924; ENSMUSG00000022523. [P61329-2]
DR   GeneID; 14167; -.
DR   KEGG; mmu:14167; -.
DR   UCSC; uc007yvr.3; mouse. [P61329-1]
DR   UCSC; uc007yvt.3; mouse. [P61329-2]
DR   CTD; 2257; -.
DR   MGI; MGI:109183; Fgf12.
DR   VEuPathDB; HostDB:ENSMUSG00000022523; -.
DR   eggNOG; KOG3885; Eukaryota.
DR   GeneTree; ENSGT00940000155929; -.
DR   HOGENOM; CLU_081609_2_0_1; -.
DR   InParanoid; P61329; -.
DR   OMA; MECKFKE; -.
DR   PhylomeDB; P61329; -.
DR   TreeFam; TF330751; -.
DR   Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR   BioGRID-ORCS; 14167; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Fgf12; mouse.
DR   PRO; PR:P61329; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P61329; protein.
DR   Bgee; ENSMUSG00000022523; Expressed in superior frontal gyrus and 167 other tissues.
DR   ExpressionAtlas; P61329; baseline and differential.
DR   Genevisible; P61329; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; ISO:MGI.
DR   GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR   GO; GO:0007254; P:JNK cascade; ISO:MGI.
DR   GO; GO:2001258; P:negative regulation of cation channel activity; ISO:MGI.
DR   GO; GO:0050905; P:neuromuscular process; IGI:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
DR   GO; GO:0003254; P:regulation of membrane depolarization; ISO:MGI.
DR   GO; GO:0098908; P:regulation of neuronal action potential; ISS:UniProtKB.
DR   GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; ISS:UniProtKB.
DR   CDD; cd00058; FGF; 1.
DR   InterPro; IPR028254; FGF12.
DR   InterPro; IPR002209; Fibroblast_GF_fam.
DR   InterPro; IPR008996; IL1/FGF.
DR   PANTHER; PTHR11486; PTHR11486; 1.
DR   PANTHER; PTHR11486:SF17; PTHR11486:SF17; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00263; HBGFFGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; SSF50353; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Growth factor; Nucleus; Reference proteome.
FT   CHAIN           1..243
FT                   /note="Fibroblast growth factor 12"
FT                   /id="PRO_0000147605"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           11..38
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..66
FT                   /note="MAAAIASSLIRQKRQARESNSDRVSASKRRSSPSKDGRSLCERHVLGVFSKV
FT                   RFCSGRKRPVRRRP -> MESK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010223"
FT   CONFLICT        42
FT                   /note="E -> D (in Ref. 2; AAB71607)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="Q -> P (in Ref. 2; AAB71607)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  27399 MW;  773ED10B5BDD033C CRC64;
     MAAAIASSLI RQKRQARESN SDRVSASKRR SSPSKDGRSL CERHVLGVFS KVRFCSGRKR
     PVRRRPEPQL KGIVTRLFSQ QGYFLQMHPD GTIDGTKDEN SDYTLFNLIP VGLRVVAIQG
     VKASLYVAMN GEGYLYSSDV FTPECKFKES VFENYYVIYS STLYRQQESG RAWFLGLNKE
     GQIMKGNRVK KTKPSSHFVP KPIEVCMYRE PSLHEIGEKQ GRSRKSSGTP TMNGGKVVNQ
     DST
 
 
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