TRI36_MOUSE
ID TRI36_MOUSE Reviewed; 729 AA.
AC Q80WG7; Q7TNM1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=E3 ubiquitin-protein ligase Trim36;
DE EC=2.3.2.27 {ECO:0000269|PubMed:19232519};
DE AltName: Full=Acrosome RBCC protein;
DE AltName: Full=Haprin {ECO:0000303|PubMed:12917430};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM36 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 36;
GN Name=Trim36;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=12917430; DOI=10.1074/jbc.m304306200;
RA Kitamura K., Tanaka H., Nishimune Y.;
RT "Haprin, a novel haploid germ cell-specific RING finger protein involved in
RT the acrosome reaction.";
RL J. Biol. Chem. 278:44417-44423(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16434393; DOI=10.1074/jbc.m512755200;
RA Short K.M., Cox T.C.;
RT "Subclassification of the RBCC/TRIM superfamily reveals a novel motif
RT necessary for microtubule binding.";
RL J. Biol. Chem. 281:8970-8980(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPH, AND CATALYTIC
RP ACTIVITY.
RX PubMed=19232519; DOI=10.1016/j.bbrc.2009.02.059;
RA Miyajima N., Maruyama S., Nonomura K., Hatakeyama S.;
RT "TRIM36 interacts with the kinetochore protein CENP-H and delays cell cycle
RT progression.";
RL Biochem. Biophys. Res. Commun. 381:383-387(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=28087737; DOI=10.1093/hmg/ddx020;
RA Singh N., Kumble Bhat V., Tiwari A., Kodaganur S.G., Tontanahal S.J.,
RA Sarda A., Malini K.V., Kumar A.;
RT "A homozygous mutation in TRIM36 causes autosomal recessive anencephaly in
RT an Indian family.";
RL Hum. Mol. Genet. 26:1104-1114(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins
CC (PubMed:19232519). Involved in chromosome segregation and cell cycle
CC regulation (PubMed:19232519). May play a role in the acrosome reaction
CC and fertilization (PubMed:12917430). {ECO:0000269|PubMed:12917430,
CC ECO:0000269|PubMed:19232519}.
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:0000269|PubMed:19232519};
CC -!- SUBUNIT: Interacts with CENPH. {ECO:0000269|PubMed:19232519}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQ86}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:12917430}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19232519}. Note=Found in the acrosomal region of
CC elongated spermatids and mature sperm (PubMed:12917430). Colocalizes
CC with alpha-tubulin (PubMed:19232519). {ECO:0000269|PubMed:12917430,
CC ECO:0000269|PubMed:19232519}.
CC -!- TISSUE SPECIFICITY: Expressed in testis (PubMed:12917430). Strongly
CC expressed in the neural tube region in 14.5 dpc embryos
CC (PubMed:28087737). {ECO:0000269|PubMed:12917430,
CC ECO:0000269|PubMed:28087737}.
CC -!- DEVELOPMENTAL STAGE: Expressed only in testicular germ cells after
CC meiotic division. Expression was first detected at the age of 4 weeks.
CC {ECO:0000269|PubMed:12917430}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC76066.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB103063; BAC76066.1; ALT_FRAME; mRNA.
DR EMBL; AY251389; AAP51209.1; -; mRNA.
DR EMBL; BC058106; AAH58106.1; -; mRNA.
DR CCDS; CCDS29229.1; -.
DR RefSeq; NP_001164326.1; NM_001170855.1.
DR RefSeq; NP_849203.2; NM_178872.4.
DR AlphaFoldDB; Q80WG7; -.
DR BioGRID; 205766; 2.
DR IntAct; Q80WG7; 1.
DR STRING; 10090.ENSMUSP00000037978; -.
DR iPTMnet; Q80WG7; -.
DR PhosphoSitePlus; Q80WG7; -.
DR EPD; Q80WG7; -.
DR MaxQB; Q80WG7; -.
DR PaxDb; Q80WG7; -.
DR PRIDE; Q80WG7; -.
DR ProteomicsDB; 298216; -.
DR Antibodypedia; 25412; 238 antibodies from 28 providers.
DR DNASU; 28105; -.
DR Ensembl; ENSMUST00000037011; ENSMUSP00000037978; ENSMUSG00000033949.
DR GeneID; 28105; -.
DR KEGG; mmu:28105; -.
DR UCSC; uc008evi.2; mouse.
DR CTD; 55521; -.
DR MGI; MGI:106264; Trim36.
DR VEuPathDB; HostDB:ENSMUSG00000033949; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158373; -.
DR HOGENOM; CLU_013137_19_3_1; -.
DR InParanoid; Q80WG7; -.
DR OMA; MYCELCK; -.
DR OrthoDB; 180330at2759; -.
DR PhylomeDB; Q80WG7; -.
DR TreeFam; TF315216; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 28105; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Trim36; mouse.
DR PRO; PR:Q80WG7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q80WG7; protein.
DR Bgee; ENSMUSG00000033949; Expressed in seminiferous tubule of testis and 137 other tissues.
DR ExpressionAtlas; Q80WG7; baseline and differential.
DR Genevisible; Q80WG7; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12894; SPRY_PRY_TRIM36; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
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; IPR027726; Trim36.
DR InterPro; IPR027370; Znf-RING_LisH.
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; PTHR24099:SF18; 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 SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 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; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Metal-binding;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..729
FT /note="E3 ubiquitin-protein ligase Trim36"
FT /id="PRO_0000056253"
FT DOMAIN 356..413
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 416..511
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 509..723
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 33..84
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 154..192
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 207..249
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..302
FT /evidence="ECO:0000255"
FT COMPBIAS 606..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT CONFLICT 292
FT /note="G -> V (in Ref. 1; BAC76066)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="N -> D (in Ref. 1; BAC76066)"
FT /evidence="ECO:0000305"
FT CONFLICT 601..602
FT /note="WL -> CV (in Ref. 1; BAC76066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 82791 MW; E13CC617EFD47F58 CRC64;
MSESEEISEF GYIMELLAKG KVTIKNIEKE LICPACKELF THPLILPCQH SVCHKCVKEL
LLSLDDSFND VASDSSNQSS PRLRLTSPSM DKIDKINRPG WKRNSLTPRP TTFPCPGCEH
DVDLGERGVS GLFRNFTLET IVERYRQAAR AATAIMCDLC KPPPQESTKS CMDCSASYCN
ECFKIYHPWG TVKAQHEYVG PTTNFRPKVL MCPEHETERI NMYCELCRRP VCHLCKLGGN
HSNHRVTTMS SAYKTLKEKL SKDIDFLIGK ESQVKSQISE LNLLMKETEC NGERAKEEAL
AHFEKLFEIL EDRKSSVLKA IDASKKLRLD KFHTQMEEYQ GLLENNGLVG YAQEVLKETD
QSCFVQTAKQ LHLRIQKATE SLKSFRPAAQ ASFEDYVVNI SKQTEVLGEL SFFSSGIDIP
EINEEQSKVY NNALIDWHHP EKDKADSYVL EYRKINRDEE MISWNEIEVH GTSKVVSNLE
SNSPYAFRVR AYRGSICSPC SRELILHTPP APVFSFLFDE KCGYNTEHLL LNLKRDRVES
RAGFNVLLAA ERIQVGHYTS LDYIIGDVGV TKGKHFWACR VEPYSYLVKV GVASSDKLQE
WLRSPRDAAS PRYEQDSGHD SGSEDACFDS SQPFTLVTIG MKKFFIPKSP TSSNEPENRV
LPMPTSIGIF LDCDKGKVSF YDMDHMKCLY ERQVDCSHTM YPAFALMGSG GIQLEEAITA
KYLEYEEDV
