ID F1RLE9_PIG Unreviewed; 724 AA.
AC F1RLE9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM36 {ECO:0000313|Ensembl:ENSSSCP00000015120.4,
GN ECO:0000313|VGNC:VGNC:94409};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000015120.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000015120.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000015120.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDC33855.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000015120.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; DQIR01278377; HDC33855.1; -; Transcribed_RNA.
DR RefSeq; XP_013850491.1; XM_013995037.1.
DR Ensembl; ENSSSCT00000015532.4; ENSSSCP00000015120.4; ENSSSCG00000014214.6.
DR GeneID; 100519890; -.
DR CTD; 55521; -.
DR VGNC; VGNC:94409; TRIM36.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158373; -.
DR OMA; EWLHSPR; -.
DR OrthoDB; 5383069at2759; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000014214; Expressed in testis and 36 other cell types or tissues.
DR Genevisible; F1RLE9; SS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19848; Bbox1_TRIM36_C-I; 1.
DR CDD; cd19778; Bbox2_TRIM36_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16756; RING-HC_TRIM36_C-I; 1.
DR CDD; cd12894; SPRY_PRY_TRIM36; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR035727; SPRY/PRY_TRIM36.
DR InterPro; IPR047066; TRIM36_Bbox1_Zfn.
DR InterPro; IPR047065; TRIM36_Bbox2_Zfn.
DR InterPro; IPR027726; Trim36_HC-RING.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24099:SF18; E3 UBIQUITIN-PROTEIN LIGASE TRIM36; 1.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1RLE9};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 21..72
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 202..244
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 351..408
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 414..506
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 491..716
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
SQ SEQUENCE 724 AA; 82510 MW; D1105C0C8381C881 CRC64;
MEGDGSDSLV TIKNIERELI CPACKELFTH PLILPCQHSI CHKCVKELLL MLDDSFNEVG
SDNSNQSSPR IRLPSPSMDK IDRISRPGHK KILNGWKRNS LTPRTTTFPC PGCEHDVDLG
ERGINGLFRN FTLETIVERY RQAARAATAI MCDLCKPPPQ ESTKSCMDCS ASYCNECFKI
YHPWGTIKAQ HEYVGPTTNF RPKILMCPEH ETERINMYCE LCRRPVCHLC KLGGNHSNHR
VTTMSSAYKT LKEKLSKDID YLIGKESQVK SQISELNLLM KETECNGERA KEEAVTHFEK
LFEVLEERKS SVLKAIDTSK KLRLDKFQTQ MEEYQGLLEN SGLVGYAQEV LKETDQSCFV
QTAKQLHLRI QKATESLKSF RPAAQTSFED YVVNTSKQTE LLGELSFFSS GVDVPEINEE
QSKIYNNALI NWYHPGKDKA DSYVLEYRKI NRDEEMLSWN ETEVFGTSKV ISDLESNCNY
AFRVRAYKGS ICSPCSRELI LHTPPAPVFS FLFDEKCGYN NEHLLLNLKR DRVESRAGFN
LLLAAERIQV GYYTSLDYII GDVGITKGKH FWAFRVEPYS YLVKVGVASS DKLQEWLRSP
RDAVSPRYEQ DSGHDSGSED ACFDSSQPFT LVTIGMKKFF IPKSPTSSNE PENRVLPMPT
SIGVFLDYDK GKVGFYDMDH MKCLYERQVD CSHTMYPAFA LMGSGGIQLE EPITAKYLEY
QENM
//
