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