FABP9_RAT
ID FABP9_RAT Reviewed; 132 AA.
AC P55054; Q68G09;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
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;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=7948479; DOI=10.1095/biolreprod51.2.239;
RA Schmitt M.C., Jamison R.S., Orgebin-Crist M.C., Ong D.E.;
RT "A novel, testis-specific member of the cellular lipophilic transport
RT protein superfamily, deduced from a complimentary deoxyribonucleic acid
RT clone.";
RL Biol. Reprod. 51:239-245(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7958448; DOI=10.1006/dbio.1994.1310;
RA Oko R., Morales C.R.;
RT "A novel testicular protein, with sequence similarities to a family of
RT lipid binding proteins, is a major component of the rat sperm perinuclear
RT theca.";
RL Dev. Biol. 166:235-245(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9283004; DOI=10.1095/biolreprod57.3.655;
RA Pouresmaeili F., Morales C.R., Oko R.;
RT "Molecular cloning and structural analysis of the gene encoding PERF 15
RT protein present in the perinuclear theca of the rat spermatozoa.";
RL Biol. Reprod. 57:655-659(1997).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14; SER-40; SER-42;
RP SER-44 AND SER-91, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- 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; U07870; AAA68627.1; -; mRNA.
DR EMBL; U09022; AAA67873.1; -; mRNA.
DR EMBL; U66878; AAB07538.1; -; Genomic_DNA.
DR EMBL; BC078817; AAH78817.1; -; mRNA.
DR PIR; I52524; I52524.
DR RefSeq; NP_074045.1; NM_022854.1.
DR AlphaFoldDB; P55054; -.
DR SMR; P55054; -.
DR BioGRID; 249200; 1.
DR STRING; 10116.ENSRNOP00000014949; -.
DR iPTMnet; P55054; -.
DR PhosphoSitePlus; P55054; -.
DR PaxDb; P55054; -.
DR GeneID; 64822; -.
DR KEGG; rno:64822; -.
DR UCSC; RGD:620285; rat.
DR CTD; 646480; -.
DR RGD; 620285; Fabp9.
DR VEuPathDB; HostDB:ENSRNOG00000011082; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P55054; -.
DR OMA; SISAVWD; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P55054; -.
DR TreeFam; TF316894; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR PRO; PR:P55054; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011082; Expressed in testis and 10 other tissues.
DR Genevisible; P55054; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
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:0001675; P:acrosome assembly; IEP:RGD.
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_0000067386"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 3
FT /note="E -> Q (in Ref. 4; AAH78817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 15089 MW; 032AB47D14D07549 CRC64;
MIEPFLGTWK LVSSENFENY VRELGVECEP RKVACLIKPS VSISFNGERM DIQAGSACRN
TEISFKLGEE FEETTADNRK VKSLITFEGG SMIQIQRWLG KQTTIKRRIV DGRMVVECTM
NNVVSTRTYE RV
