ID A0A1S3FPV7_DIPOR Unreviewed; 578 AA.
AC A0A1S3FPV7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protein fem-1 homolog A {ECO:0000313|RefSeq:XP_012878059.1};
GN Name=Fem1a {ECO:0000313|RefSeq:XP_012878059.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012878059.1};
RN [1] {ECO:0000313|RefSeq:XP_012878059.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012878059.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the fem-1 family.
CC {ECO:0000256|ARBA:ARBA00038500}.
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DR RefSeq; XP_012878059.1; XM_013022605.1.
DR AlphaFoldDB; A0A1S3FPV7; -.
DR STRING; 10020.ENSDORP00000021367; -.
DR GeneID; 105990243; -.
DR KEGG; dord:105990243; -.
DR CTD; 55527; -.
DR InParanoid; A0A1S3FPV7; -.
DR OMA; ENKIGHE; -.
DR OrthoDB; 1063832at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0031867; F:EP4 subtype prostaglandin E2 receptor binding; IEA:Ensembl.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IEA:Ensembl.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24173; ANKYRIN REPEAT CONTAINING; 1.
DR PANTHER; PTHR24173:SF74; UVEAL AUTOANTIGEN WITH COILED-COIL DOMAINS AND ANKYRIN REPEATS; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 6.
DR PROSITE; PS50088; ANK_REPEAT; 6.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT REPEAT 40..61
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 74..106
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 107..139
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 139..161
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 443..488
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 489..521
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 161..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 63750 MW; CF8CBB1351563221 CRC64;
MDLHTAVYNA ARDGKLQLLQ KLLGGRGREE LEELMGAAAG GGTPLLIAAR RGHLDVVRYL
VGEHQADLEV ANRHGHTCLM ISCYKGHREI ARYLLEQGAR VNRRSAKGNT ALHDCAESGS
LEILQLLLGR RARMERDGYG MTPLLAASVT GHTNIVEFLI QAQPGLERPP RSPGGPEDPE
DDEEEQRDPD APSVESCCPT SREAAVEALE LLGATYVDKK RDLLGALKHW RRAMELRHQG
GEYLPKPQPP QLVLAYGYAR EVSTVQELEA LITDPDEMRM QALLIRERIL GPSHPDTSYY
IRYRGAVYAD SGNFQRCIGL WKYALDMQQN HLEPLSPMTA SSFLSFAELF SYVLQERSAK
APGPGPHVGF ADLMGVLGKG VREVERALQL PKEPGDAGQF AKALAIILHL LYLLEKVECS
PSQEHLKHQT VYRLLKCAPR GKNGFTPLHM AVDKDTTHVG RYRVGLFPSL AVVRVLLDCG
ADPDSRDFDN NTPLHIAAQN NCPAIMSALV EAGAHLDTTN AFRKTPLELL AGELLAAGAL
QPFNHVSLQC LAARALHRNK VPYKGFIPED LEAFIELH
//
