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FABP9_MOUSE
ID   FABP9_MOUSE             Reviewed;         132 AA.
AC   O08716; Q9DAL2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Fatty acid-binding protein 9;
DE   AltName: Full=15 kDa perforatorial protein;
DE            Short=PERF 15;
DE   AltName: Full=Testis lipid-binding protein;
DE            Short=TLBP;
DE   AltName: Full=Testis-type fatty acid-binding protein;
DE            Short=T-FABP;
GN   Name=Fabp9; Synonyms=Perf15, Tlbp;
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].
RC   STRAIN=CD-1; TISSUE=Testis;
RX   PubMed=9408250; DOI=10.1095/biolreprod57.6.1426;
RA   Korley R., Pouresmaeili F., Oko R.;
RT   "Analysis of the protein composition of the mouse sperm perinuclear theca
RT   and characterization of its major protein constituent.";
RL   Biol. Reprod. 57:1426-1432(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; U96149; AAB53798.1; -; mRNA.
DR   EMBL; AK005745; BAB24218.1; -; mRNA.
DR   EMBL; AK161314; BAE36318.1; -; mRNA.
DR   EMBL; BC048437; AAH48437.1; -; mRNA.
DR   CCDS; CCDS17237.1; -.
DR   RefSeq; NP_035728.2; NM_011598.3.
DR   AlphaFoldDB; O08716; -.
DR   SMR; O08716; -.
DR   STRING; 10090.ENSMUSP00000029038; -.
DR   iPTMnet; O08716; -.
DR   PhosphoSitePlus; O08716; -.
DR   REPRODUCTION-2DPAGE; IPI00396813; -.
DR   jPOST; O08716; -.
DR   MaxQB; O08716; -.
DR   PaxDb; O08716; -.
DR   PeptideAtlas; O08716; -.
DR   PRIDE; O08716; -.
DR   ProteomicsDB; 271549; -.
DR   DNASU; 21884; -.
DR   Ensembl; ENSMUST00000029038; ENSMUSP00000029038; ENSMUSG00000027528.
DR   GeneID; 21884; -.
DR   KEGG; mmu:21884; -.
DR   UCSC; uc008opj.2; mouse.
DR   CTD; 646480; -.
DR   MGI; MGI:1194881; Fabp9.
DR   VEuPathDB; HostDB:ENSMUSG00000027528; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000161845; -.
DR   HOGENOM; CLU_113772_0_0_1; -.
DR   InParanoid; O08716; -.
DR   OMA; KMMTIRT; -.
DR   OrthoDB; 1417203at2759; -.
DR   PhylomeDB; O08716; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-MMU-163560; Triglyceride catabolism.
DR   BioGRID-ORCS; 21884; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Fabp9; mouse.
DR   PRO; PR:O08716; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; O08716; protein.
DR   Bgee; ENSMUSG00000027528; Expressed in seminiferous tubule of testis and 28 other tissues.
DR   ExpressionAtlas; O08716; baseline and differential.
DR   Genevisible; O08716; MM.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; PTHR11955; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lipid-binding; Phosphoprotein; Reference proteome; Transport.
FT   CHAIN           1..132
FT                   /note="Fatty acid-binding protein 9"
FT                   /id="PRO_0000067385"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55054"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55054"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55054"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55054"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55054"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55054"
FT   CONFLICT        12
FT                   /note="I -> V (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="E -> K (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="V -> I (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="K -> R (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="K -> R (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="K -> R (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="I -> T (in Ref. 1; AAB53798)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   132 AA;  15017 MW;  D52B2279F0A7E272 CRC64;
     MIEPFLGTWK LISSENFENY VRELGVECEP RKVACLIKPS VSISFNGERM DIQAGSACRN
     TEISFKLGEE FEETTADNRK VKSLITFEGG SMIQVQKWLG KQTTIKRKIV DGKMVVECTM
     NNVVSTRIYE RV
 
 
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