PEX13_BOVIN
ID PEX13_BOVIN Reviewed; 403 AA.
AC Q0P5B1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Peroxisomal membrane protein PEX13;
DE AltName: Full=Peroxin-13;
GN Name=PEX13;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX14 and PEX17. Functions as a docking factor for the predominantly
CC cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1
CC and PTS2 proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PEX19. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxin-13 family. {ECO:0000305}.
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DR EMBL; BC120277; AAI20278.1; -; mRNA.
DR RefSeq; NP_001069680.1; NM_001076212.2.
DR AlphaFoldDB; Q0P5B1; -.
DR SMR; Q0P5B1; -.
DR STRING; 9913.ENSBTAP00000006917; -.
DR PaxDb; Q0P5B1; -.
DR PRIDE; Q0P5B1; -.
DR Ensembl; ENSBTAT00000006917; ENSBTAP00000006917; ENSBTAG00000005257.
DR GeneID; 540337; -.
DR KEGG; bta:540337; -.
DR CTD; 5194; -.
DR VEuPathDB; HostDB:ENSBTAG00000005257; -.
DR VGNC; VGNC:32755; PEX13.
DR eggNOG; KOG3875; Eukaryota.
DR GeneTree; ENSGT00390000016883; -.
DR HOGENOM; CLU_045457_0_0_1; -.
DR InParanoid; Q0P5B1; -.
DR OMA; QPKIRGW; -.
DR OrthoDB; 1085263at2759; -.
DR TreeFam; TF327117; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000005257; Expressed in spermatocyte and 106 other tissues.
DR ExpressionAtlas; Q0P5B1; baseline.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0060152; P:microtubule-based peroxisome localization; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; ISS:UniProtKB.
DR GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
DR InterPro; IPR007223; Peroxin-13_N.
DR InterPro; IPR035463; Pex13.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR19332; PTHR19332; 1.
DR Pfam; PF04088; Peroxin-13_N; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Membrane; Peroxisome; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..403
FT /note="Peroxisomal membrane protein PEX13"
FT /id="PRO_0000371413"
FT TOPO_DOM 1..233
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 272..336
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0K1"
SQ SEQUENCE 403 AA; 44361 MW; 38F77CF4EA030A97 CRC64;
MASQPPPPPK PWETRRIPGT GPGPGPGPTF QSAELGPTLL TRPGQPTLTR VPPPILPRPS
QQTGSGNLNT FRPAYSSFSS GYGAYGNSFY GSYSPYSYGY NGLGYNRLRI DDLPPSRFVQ
QAEESSRGAF QSIESIVHAF ASVSMMMDAT FSAVYNSFRA VLDVANHFSR LKIHFTKVFS
AFALVRTIRY LYRRLQWMIG LRRGLENEDL WAESEGTVAC LGAEDRAANS AKSWPIFLFF
AVILGGPYLI WKLLSTHSDE VTDSTNWASG EDDHVVARAE YDFVAVSEEE ISFRAGDMLN
LALKEQQPRV RGWLLASLDG QTTGLIPANY VKILGKRRGR KTVESSRISK QQQSFTNTTL
IKGATAADSL DDQEAAFESV FVETNKVPVA SDSTGKNGDK QDL