ID F2PPM5_TRIEC Unreviewed; 822 AA.
AC F2PPM5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Extracellular membrane protein CFEM domain-containing protein {ECO:0000259|Pfam:PF05730};
GN ORFNames=TEQG_02877 {ECO:0000313|EMBL:EGE03843.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-
CC anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the RBT5 family.
CC {ECO:0000256|ARBA:ARBA00010031}.
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DR EMBL; DS995729; EGE03843.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PPM5; -.
DR VEuPathDB; FungiDB:TEQG_02877; -.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_344237_0_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008427; Extracellular_membr_CFEM_dom.
DR PANTHER; PTHR37456:SF5; -; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF05730; CFEM; 1.
DR Pfam; PF01391; Collagen; 3.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..822
FT /note="Extracellular membrane protein CFEM domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003283706"
FT DOMAIN 605..668
FT /note="Extracellular membrane protein CFEM"
FT /evidence="ECO:0000259|Pfam:PF05730"
FT REGION 465..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 81525 MW; 76B2AA1A55222712 CRC64;
MKASVGALAL LLAQQASAAY IPSGSDKGSA LVRRGWDGFD GGEQTVDTGF NGNWGQEPCE
NCGGGGGVPD CPDGNCGGGG VPQCPDGNCG GGVPDCPDGN CGGGGVPQCP DGNCGNTGGN
IGGEIGGNIG GGIGGGIGGG GWWGGHNGMP PVCYPVPGNT VPDCTPEQHG GFDWIGLIEG
AIEFFGGCDF TGFTCVDGFF KGALEIGGKV ITALLRAGDG NAPTISRPEG ALTITTIEIV
AEVEVEIVLE FSMSDGSICR QFASCGPSLT TVVNEQCGGA VSVSFHLAVH SKVSVCAVAI
KKINFGCEPP TIPTLPFPTS FPTPSLPPPE TPVPSISWST GYTTIPGTSE SGSWSVPPAV
TNTMPSYSMP TSGYTTVPGP VPSSSIPSGG FPTTGSGGIP GQTTVPSSPA PTTWITQSTS
TVFTTSTMTI TSCPPDVPNC PTGSTTVITS TVPVYTTICP VTMTTAIPGQ PGQPGQPGQP
GQPGQPGQPG QPGQPGQPGQ PGQPGQPGQP GQPGQPGQPG QPGQPGQPGQ PGQPGQPGQP
GQPGQPGQPG QPGQPGQPGQ PGQPGQPGQP GQPGQPGQPG QPGQPGQPGQ PGQPGQPGAP
APPPASYPPV VPNCMITWFT IPKCDSNSDI KCLCPSPEFA HKVVSCIQAW STSEHETQAA
LSFFLGICVS YIPQNPGLVD HLPPGMPIAP APVSSGPAPP VVTLTITPTM TSGNGTVPPT
TIVVPPISFA PPVSGAPGPY PVPAGPTSDG GSIPTPAPGG VPPAAPPYGS TGFMTVSPTG
GVPHPTSTTE PYIGAASSVE GFLSQWVMMG ITAMVGLIQF AL
//
