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TBC14_RAT
ID   TBC14_RAT               Reviewed;         694 AA.
AC   Q5CD77; Q499U3; Q6I7R4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=TBC1 domain family member 14;
DE   AltName: Full=Spermatogenesis-related factor 2;
DE            Short=SRF-2;
DE   AltName: Full=Up-regulated in nephrectomized rat kidney #2;
GN   Name=Tbc1d14; ORFNames=UR-NR#2;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=15758561; DOI=10.1507/endocrj.52.75;
RA   Yamano Y., Ohyama K., Ohta M., Sano T., Ritani A., Shimada J., Ashida N.,
RA   Yoshida E., Ikehara K., Morishima I.;
RT   "A novel spermatogenesis related factor-2 (SRF-2) gene expression affected
RT   by TCDD treatment.";
RL   Endocr. J. 52:75-81(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 278-694, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Wistar; TISSUE=Kidney;
RX   PubMed=15200410; DOI=10.1111/j.1523-1755.2004.00704.x;
RA   Horiba N., Masuda S., Takeuchi A., Saito H., Okuda M., Inui K.;
RT   "Gene expression variance based on random sequencing in rat remnant
RT   kidney.";
RL   Kidney Int. 66:29-45(2004).
CC   -!- FUNCTION: Plays a role in the regulation of starvation-induced
CC       autophagosome formation. Together with the TRAPPIII complex, regulates
CC       a constitutive trafficking step from peripheral recycling endosomes to
CC       the early Golgi, maintaining the cycling pool of ATG9 required for
CC       initiation of autophagy. {ECO:0000250|UniProtKB:Q9P2M4}.
CC   -!- SUBUNIT: Interacts with ULK1. May interact with RAB11A and RAB11B, but
CC       does not exhibit any GTPase-activating activity toward these proteins.
CC       Interacts with TRAPPC8. {ECO:0000250|UniProtKB:Q9P2M4}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC       {ECO:0000250|UniProtKB:Q9P2M4}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:Q9P2M4}. Note=After amino acid starvation, Golgi
CC       apparatus-associated protein levels increase compared with fed
CC       conditions. May be cycling between the Golgi apparatus and an endosomal
CC       pool, redistributing to the Golgi apparatus upon starvation.
CC       {ECO:0000250|UniProtKB:Q9P2M4}.
CC   -!- TISSUE SPECIFICITY: PubMed:15758561 detected expression at the stage of
CC       sexual maturation in testis, mainly in the spermatocytes. No expression
CC       detected in the ovary, brain, heart, lung, liver and kidney.
CC       PubMed:15200410 detected expression in brain, heart, lung, liver,
CC       spleen and kidney but not in small intestine.
CC       {ECO:0000269|PubMed:15200410, ECO:0000269|PubMed:15758561}.
CC   -!- DEVELOPMENTAL STAGE: First detected in the testis at 5 weeks. Level of
CC       expression increases up to 7 weeks and maintains even at 63 weeks.
CC       {ECO:0000269|PubMed:15758561}.
CC   -!- INDUCTION: Up-regulated in nephrectomized kidney.
CC       {ECO:0000269|PubMed:15200410}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH99760.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD23893.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD91010.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD91010.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB117752; BAD91010.1; ALT_SEQ; mRNA.
DR   EMBL; BC099760; AAH99760.1; ALT_INIT; mRNA.
DR   EMBL; AB108668; BAD23893.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001012152.2; NM_001012152.2.
DR   RefSeq; NP_001029193.2; NM_001034021.2.
DR   RefSeq; NP_001106836.1; NM_001113365.1.
DR   AlphaFoldDB; Q5CD77; -.
DR   SMR; Q5CD77; -.
DR   STRING; 10116.ENSRNOP00000055215; -.
DR   PhosphoSitePlus; Q5CD77; -.
DR   PaxDb; Q5CD77; -.
DR   GeneID; 360956; -.
DR   KEGG; rno:360956; -.
DR   CTD; 57533; -.
DR   RGD; 1309993; Tbc1d14.
DR   eggNOG; KOG2223; Eukaryota.
DR   InParanoid; Q5CD77; -.
DR   OrthoDB; 798837at2759; -.
DR   PhylomeDB; Q5CD77; -.
DR   Reactome; R-RNO-8854214; TBC/RABGAPs.
DR   PRO; PR:Q5CD77; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005776; C:autophagosome; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR   GO; GO:0071955; P:recycling endosome to Golgi transport; ISO:RGD.
DR   GO; GO:2000785; P:regulation of autophagosome assembly; ISO:RGD.
DR   InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR   InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR   Pfam; PF00566; RabGAP-TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; SSF47923; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; GTPase activation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..694
FT                   /note="TBC1 domain family member 14"
FT                   /id="PRO_0000319418"
FT   DOMAIN          402..612
FT                   /note="Rab-GAP TBC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT   REGION          108..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2M4"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2M4"
FT   CONFLICT        278..282
FT                   /note="KKTQK -> GLASM (in Ref. 3; BAD23893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="N -> S (in Ref. 3; BAD23893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="I -> M (in Ref. 3; BAD23893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        420
FT                   /note="L -> V (in Ref. 3; BAD23893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="L -> F (in Ref. 3; BAD23893)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   694 AA;  78209 MW;  6DAE2A6B5F47AA1F CRC64;
     MTDGNLSTSM NGVALMGILD GRPGDSLQEL QHLSIKAVPR SLSVPDYGPT LKLGALEDRH
     SLQSVDSGIP TLEIGNPEPV PCSVVHVKRK QSESEIIPER AFQSACPLPS CTPSAPTGSE
     REQAVRKSST FPRTGYDSVK LYSPTSKALS RSDDVSVCSV SSLGTELSTT LSVSNEDILD
     LMVTSNSSAI VTLENDDDPQ FTDVTLSSIK ETSDLHQQDC VAETEEGRKL RLLQPFSHFF
     TRNLLARKQN ARLDRQRDLG WKLFGKVPLR ETAQKDSKKT QKEYEDKAGR PSRPPSPKQN
     VRKNLDFEPL STTALILEDR PANLPAKPAE EAQKHRQQYE EMVVQAKKRE LKEAQRRKKQ
     LEERCKVEES IGNAVLTWNN EILPNWETMW CSKKVRDLWW QGIPPSVRGK VWSLAIGNEL
     NITHELFDIC LARAKERWRS LSTGGSEVEN EDAGFSAADR EASLELIKLD ISRTFPNLCI
     FQQGGPYHDM LHSILGAYTC YRPDVGYVQG MSFIAAVLIL NLDTADAFIA FSNLLNKPCQ
     MAFFRVDHGL MLTYFAAFEV FFEENLPKLF AHFKKNNLTA DIYLIDWIFT LYSKSLPLDL
     ACRIWDVFCR DGEEFLFRTA LGILKLFEDI LTRMDFIHSA QFLTRLPEDL PADDVFAAIS
     TVQMQSRNKK WAQVLSALQK DSREMEEGSP SVRD
 
 
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