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Database: UniProt
Entry: F2PQU9_TRIEC
LinkDB: F2PQU9_TRIEC
Original site: F2PQU9_TRIEC 
ID   F2PQU9_TRIEC            Unreviewed;       475 AA.
AC   F2PQU9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Peroxisome assembly protein 12 {ECO:0000256|ARBA:ARBA00018980};
DE   AltName: Full=Peroxin-12 {ECO:0000256|ARBA:ARBA00029692};
GN   ORFNames=TEQG_03297 {ECO:0000313|EMBL:EGE04267.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel,
CC       composed of PEX2, PEX10 and PEX12. {ECO:0000256|ARBA:ARBA00034505}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC       membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004585}.
CC   -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family.
CC       {ECO:0000256|ARBA:ARBA00008704}.
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DR   EMBL; DS995732; EGE04267.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PQU9; -.
DR   VEuPathDB; FungiDB:TEQG_03297; -.
DR   eggNOG; KOG0826; Eukaryota.
DR   HOGENOM; CLU_031067_2_1_1; -.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017375; PEX12.
DR   InterPro; IPR006845; Pex_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12888:SF0; PEROXISOME ASSEMBLY PROTEIN 12; 1.
DR   PANTHER; PTHR12888; PEROXISOME ASSEMBLY PROTEIN 12 PEROXIN-12; 1.
DR   Pfam; PF04757; Pex2_Pex12; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          378..459
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|SMART:SM00184"
FT   REGION          425..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  53286 MW;  F2C842DD382D5ECB CRC64;
     MEYMSSLQNN FDDFKPSLFE LLSEQQLSSL LPPSLRYLLA VATHRHPRYL LRILNSYDEL
     YALVSLLVEG YYLRNFGGSF TENFYSLKRE RVLALRDGEV PRAQLGAGGP VRETLKLRDS
     DIWRNLVIMV GIPYLKRKLD EGYDIHAAPH AALVSGMGGG PRYHPSDELP HNPTMKQRLL
     FYYKRFLRNV YPSINGAYYF SILAFNLAYL FDNTKYSSPF LWLIGTRIRR LSPADHKAIA
     MATAANTPHT GASRSRSRPS ALSLLNPQAI YPHLLGSLKI LLPASIFALK FLEWWHASDF
     SRQLAKQATQ SIELPAPVVT GIPSKSISTG SKSEKAMLAE IERPKQCRTK SPISSITLLP
     IFTVPIPPVD PDTSQAPCPI CLNPLVNPTA CQTGYVYCYT CIFRWLNGEH DRQIDFMNGA
     GNGAAWEDDD KDDENEKSGK ASTSREGRWE NGKGRCPITG RRVLGGTDGL RRVLV
//
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