ID G1P3L9_MYOLU Unreviewed; 571 AA.
AC G1P3L9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Autocrine motility factor receptor {ECO:0000313|Ensembl:ENSMLUP00000004521.2};
GN Name=AMFR {ECO:0000313|Ensembl:ENSMLUP00000004521.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000004521.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000004521.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000004521.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AAPE02054862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006106795.1; XM_006106733.2.
DR AlphaFoldDB; G1P3L9; -.
DR STRING; 59463.ENSMLUP00000004521; -.
DR Ensembl; ENSMLUT00000004959.2; ENSMLUP00000004521.2; ENSMLUG00000004958.2.
DR GeneID; 102438292; -.
DR KEGG; mlf:102438292; -.
DR CTD; 267; -.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00940000156482; -.
DR HOGENOM; CLU_015061_0_0_1; -.
DR InParanoid; G1P3L9; -.
DR OMA; WAWFTAL; -.
DR OrthoDB; 2912447at2759; -.
DR TreeFam; TF320052; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:1904288; F:BAT3 complex binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:2000638; P:regulation of SREBP signaling pathway; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR CDD; cd14421; CUE_AMFR; 1.
DR CDD; cd16455; RING-H2_AMFR; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040675; AMFR_Ube2g2-bd.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15067:SF4; E3 UBIQUITIN-PROTEIN LIGASE AMFR; 1.
DR PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR Pfam; PF02845; CUE; 1.
DR Pfam; PF18442; G2BR; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..308
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 385..427
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT REGION 428..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 65145 MW; DBAC15E19FEAA9A2 CRC64;
DVAQYLLSDS LFVWVLVNTA CCVLMLMAKL IQCIVFGPLR VSERQHLKDK FWNFIFYKFI
FIFGVLNVQT VGEVVMWCLW FAGLVFLHLM VQLCKDRFEY LSFSPTTPMS SHGRVLSLLM
AMLLSCCGLA VICCVTGYIH GMHTLAFMAV ESLLVTVRTA HVILRYVIHL WDLNHEGTWE
GKGTYVYYTD FVMELTLLSL DLMHHIHMLL FGNIWLSMAS LVIFMQLRYL FHEVQRRIRR
HKNYLHVVGN MEARFAVATP EELAVNNDDC AICWDSMQAA RKLPCGHLFH NSCLRSWLEQ
DTSCPTCRMS LNIADNNRVR EDHPGENLDE NLVPVAAAEG RPRLNQHNHF FHFDGSRIAS
WLPSFSVEVM HTTNILGITQ ASNSQLNAMA HQIQEMFPQV PYPLVLQDLQ LTRSVEITTD
NILEGRIQVP FPTQRSDGIR PALNSPDRPN SDLDEGETAA QAERMPLALS PRLEEALDFS
EVEAEPGEGE DFEARGSRFS KSADERQRML VQRKDDLLQQ ARKRFLNRSS EDDSASESCL
ASEGTASDPV TLRRRMLAAA AERRLQKQQT S
//
