ID TRIM3_HUMAN Reviewed; 744 AA.
AC O75382; B7Z5E6; F5H2Q8; Q4V9L4; Q9C038; Q9C039;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 01-MAY-2013, entry version 123.
DE RecName: Full=Tripartite motif-containing protein 3;
DE AltName: Full=Brain-expressed RING finger protein;
DE AltName: Full=RING finger protein 22;
DE AltName: Full=RING finger protein 97;
GN Name=TRIM3; Synonyms=BERP, RNF22, RNF97;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Brain;
RX PubMed=11170753; DOI=10.1006/geno.2000.6452;
RA El-Husseini A.E.-D., Fretier P., Vincent S.R.;
RT "Cloning and characterization of a gene (RNF22) encoding a novel brain
RT expressed ring finger protein (BERP) that maps to human chromosome
RT 11p15.5.";
RL Genomics 71:363-367(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA Minucci S., Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Cervix;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION IN THE CART COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15772161; DOI=10.1091/mbc.E04-11-1014;
RA Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.;
RT "CART: an Hrs/actinin-4/BERP/myosin V protein complex required for
RT efficient receptor recycling.";
RL Mol. Biol. Cell 16:2470-2482(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP INTERACTION WITH ZFYVE28.
RX PubMed=19460345; DOI=10.1016/j.devcel.2009.03.015;
RA Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,
RA Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.;
RT "Monoubiquitinylation regulates endosomal localization of Lst2, a
RT negative regulator of EGF receptor signaling.";
RL Dev. Cell 16:687-698(2009).
CC -!- FUNCTION: Probably involved in vesicular trafficking via its
CC association with the CART complex. The CART complex is necessary
CC for efficient transferrin receptor recycling but not for EGFR
CC degradation.
CC -!- SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4
CC (ACTN4) (By similarity). Component of the CART complex, at least
CC composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with
CC ZFYVE28/LST2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha;
CC IsoId=O75382-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O75382-2; Sequence=VSP_005758;
CC Name=Gamma;
CC IsoId=O75382-3; Sequence=VSP_005759;
CC Name=4;
CC IsoId=O75382-4; Sequence=VSP_044780, VSP_044781;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, uterus and testis.
CC -!- DOMAIN: The interaction with MYO5B is dependent upon its NHL
CC repeats, which form a beta-propeller (NHL) domain containing six
CC blades (By similarity).
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC -!- SIMILARITY: Contains 1 filamin repeat.
CC -!- SIMILARITY: Contains 6 NHL repeats.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR EMBL; AF045239; AAC24809.1; -; mRNA.
DR EMBL; AF220020; AAG53474.1; -; mRNA.
DR EMBL; AF220021; AAG53475.1; -; mRNA.
DR EMBL; AF220022; AAG53476.1; -; mRNA.
DR EMBL; AK291396; BAF84085.1; -; mRNA.
DR EMBL; AK298843; BAH12882.1; -; mRNA.
DR EMBL; AC084337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68709.1; -; Genomic_DNA.
DR EMBL; BC096827; AAH96827.1; -; mRNA.
DR IPI; IPI00152001; -.
DR IPI; IPI00216078; -.
DR IPI; IPI00985414; -.
DR IPI; IPI01014134; -.
DR RefSeq; NP_001234935.1; NM_001248006.1.
DR RefSeq; NP_001234936.1; NM_001248007.1.
DR RefSeq; NP_006449.2; NM_006458.3.
DR RefSeq; NP_150594.2; NM_033278.3.
DR UniGene; Hs.591992; -.
DR ProteinModelPortal; O75382; -.
DR IntAct; O75382; 3.
DR STRING; 9606.ENSP00000340797; -.
DR PhosphoSite; O75382; -.
DR PaxDb; O75382; -.
DR PRIDE; O75382; -.
DR Ensembl; ENST00000345851; ENSP00000340797; ENSG00000110171.
DR Ensembl; ENST00000359518; ENSP00000352508; ENSG00000110171.
DR Ensembl; ENST00000525074; ENSP00000433102; ENSG00000110171.
DR Ensembl; ENST00000536344; ENSP00000445460; ENSG00000110171.
DR GeneID; 10612; -.
DR KEGG; hsa:10612; -.
DR UCSC; uc001mdh.3; human.
DR CTD; 10612; -.
DR GeneCards; GC11M006469; -.
DR HGNC; HGNC:10064; TRIM3.
DR HPA; HPA043396; -.
DR HPA; HPA048233; -.
DR MIM; 605493; gene.
DR neXtProt; NX_O75382; -.
DR PharmGKB; PA35534; -.
DR eggNOG; COG3391; -.
DR HOGENOM; HOG000220817; -.
DR HOVERGEN; HBG054843; -.
DR InParanoid; O75382; -.
DR KO; K11997; -.
DR OMA; CESCLQN; -.
DR OrthoDB; EOG46T30V; -.
DR PhylomeDB; O75382; -.
DR GenomeRNAi; 10612; -.
DR NextBio; 40314; -.
DR ArrayExpress; O75382; -.
DR Bgee; O75382; -.
DR CleanEx; HS_TRIM3; -.
DR Genevestigator; O75382; -.
DR GermOnline; ENSG00000110171; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001298; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR013017; NHL_repeat_subgr.
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 Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; Ig_E-set; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
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 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Endosome; Metal-binding; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1 744 Tripartite motif-containing protein 3.
FT /FTId=PRO_0000056197.
FT REPEAT 317 418 Filamin.
FT REPEAT 473 516 NHL 1.
FT REPEAT 520 563 NHL 2.
FT REPEAT 564 605 NHL 3.
FT REPEAT 609 652 NHL 4.
FT REPEAT 656 699 NHL 5.
FT REPEAT 700 743 NHL 6.
FT ZN_FING 22 63 RING-type.
FT ZN_FING 110 151 B box-type.
FT COILED 153 224 Potential.
FT MOD_RES 7 7 Phosphoserine (By similarity).
FT VAR_SEQ 1 119 Missing (in isoform 4).
FT /FTId=VSP_044780.
FT VAR_SEQ 120 120 G -> M (in isoform 4).
FT /FTId=VSP_044781.
FT VAR_SEQ 146 156 Missing (in isoform Beta).
FT /FTId=VSP_005758.
FT VAR_SEQ 224 302 Missing (in isoform Gamma).
FT /FTId=VSP_005759.
FT VARIANT 298 298 L -> R (in dbSNP:rs10128723).
FT /FTId=VAR_052124.
FT CONFLICT 113 113 L -> F (in Ref. 1; AAC24809 and 2;
FT AAG53474/AAG53475/AAG53476).
FT CONFLICT 236 236 S -> T (in Ref. 1; AAC24809 and 2;
FT AAG53474/AAG53475).
FT CONFLICT 347 347 T -> A (in Ref. 1; AAC24809 and 2;
FT AAG53474/AAG53475/AAG53476).
FT CONFLICT 450 450 V -> L (in Ref. 3; BAH12882).
FT CONFLICT 631 631 N -> S (in Ref. 1; AAC24809 and 2;
FT AAG53474/AAG53475/AAG53476).
FT CONFLICT 636 636 I -> V (in Ref. 1; AAC24809 and 2;
FT AAG53474/AAG53475/AAG53476).
FT CONFLICT 646 646 V -> E (in Ref. 1; AAC24809 and 2;
FT AAG53474/AAG53475/AAG53476).
SQ SEQUENCE 744 AA; 80830 MW; FF9829CB52314DD2 CRC64;
MAKREDSPGP EVQPMDKQFL VCSICLDRYQ CPKVLPCLHT FCERCLQNYI PAQSLTLSCP
VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPDGAHDPE DPHPLSVVAG RPLSCPNHEG
KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLETICGAK QKVLQSQLDT
LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
ELRAEITGPD GTRLPVPVVD HKNGTYELVY TARTEGELLL SVLLYGQPVR GSPFRVRALR
PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG
REKGEFTNLQ GVSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA
VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
LTSDGHVVVA DAGNHCFKAY RYLQ
//
