ID   ATCAY_MACFA             Reviewed;         371 AA.
AC   Q9GKT0;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Caytaxin;
GN   Name=ATCAY; ORFNames=QccE-20783;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in the development of neural tissues, particularly
CC       the postnatal maturation of the cerebellar cortex. May play a role in
CC       neurotransmission through regulation of glutaminase/GLS, an enzyme
CC       responsible for the production in neurons of the glutamate
CC       neurotransmitter. Alternatively, may regulate the localization of
CC       mitochondria within axons and dendrites (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with KLC1; may link mitochondria to KLC1 and
CC       regulate mitochondria localization into neuron projections. Interacts
CC       with GLS; the interaction is direct and may control GLS localization,
CC       negatively regulating its activity. Interacts with PIN1 (via WW
CC       domain); upon NGF stimulation. The interaction with PIN1 and GLS is
CC       competitive. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q1M168}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q1M168}. Presynapse
CC       {ECO:0000250|UniProtKB:Q8BHE3}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q1M168}. Cell projection, growth cone
CC       {ECO:0000250|UniProtKB:Q1M168}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q86WG3}.
CC   -!- DOMAIN: The CRAL-TRIO domain is known to bind small hydrophobic
CC       molecules. {ECO:0000250}.
CC   -!- PTM: Cleaved by CASP3 and CASP7. The potential C-terminal product
CC       released by CASP3 cleavage may inhibit the ERK signaling pathway
CC       through MAP2K2 (By similarity). {ECO:0000250}.
CC   -!- PTM: May be ubiquitinated by STUB1. {ECO:0000250}.
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DR   EMBL; AB052149; BAB19004.1; -; mRNA.
DR   RefSeq; NP_001306294.1; NM_001319365.1.
DR   AlphaFoldDB; Q9GKT0; -.
DR   STRING; 9541.XP_005587593.1; -.
DR   GeneID; 102138092; -.
DR   CTD; 85300; -.
DR   eggNOG; KOG3308; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
DR   GO; GO:2000212; P:negative regulation of glutamate metabolic process; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0035418; P:protein localization to synapse; ISS:UniProtKB.
DR   GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; -; 1.
DR   InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   Pfam; PF12496; BNIP2; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; SSF52087; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Mitochondrion; Neurogenesis;
KW   Reference proteome; Synapse; Transport; Ubl conjugation.
FT   CHAIN           1..371
FT                   /note="Caytaxin"
FT                   /id="PRO_0000210768"
FT   DOMAIN          171..328
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..120
FT                   /note="Required for interaction with KLC1"
FT                   /evidence="ECO:0000250"
FT   REGION          190..371
FT                   /note="Mediates interaction with GLS"
FT                   /evidence="ECO:0000250"
FT   REGION          331..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            105..106
FT                   /note="Cleavage; by CASP3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  42020 MW;  2E729596E3EB2010 CRC64;
     MGTTEATLRM ENVDVKEEWQ DEDLPRPLPE ETGVELLGSP VEDTSSPPNT LNFNGAHRKR
     KTLVAPDINI SLDQSEGSLL SDDFLDTPDD LDINVDDIET PDETDSLEFL GNGNELEWGD
     DTPVATAKNM PGDSADLFGD GTTEDGGAAN GRLWRTVIIG EQEHRIDLHM IRPYMKVVTH
     GGYYGEGLNA IIVFAACFLP DSSLPDYHYI MENLFLYVIS SLELLVAEDY MIVYLNGATP
     RRRMPGIGWL KKCYQMIDRR LRKNLKSLII VHPSWFIRTV LAISRPFISV KFINKIQYVH
     SLEDLEQLIP MEHVQIPDCV LQYEEERLKA RRESARPQPE FVMPRSEEKP EVAPVENRSA
     PVTEDQETSM S