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Database: UniProt
Entry: Q6PAV2
LinkDB: Q6PAV2
Original site: Q6PAV2 
ID   HERC4_MOUSE             Reviewed;        1057 AA.
AC   Q6PAV2; Q3UL34; Q3UPX2; Q810A0; Q811C9; Q8R315; Q9D797;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   19-MAR-2014, entry version 80.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HERC4;
DE            EC=6.3.2.-;
DE   AltName: Full=HECT domain and RCC1-like domain-containing protein 4;
GN   Name=Herc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Blastocyst, Eye, Melanocyte, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, FVB/N, and FVB/N-3;
RC   TISSUE=Brain, Colon, and Mammary tumor;
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   [3]
RP   FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=129/Ola, and C57BL/6;
RX   PubMed=17967448; DOI=10.1016/j.ydbio.2007.09.053;
RA   Rodriguez C.I., Stewart C.L.;
RT   "Disruption of the ubiquitin ligase HERC4 causes defects in
RT   spermatozoon maturation and impaired fertility.";
RL   Dev. Biol. 312:501-508(2007).
RN   [4]
RP   MISCELLANEOUS.
RX   PubMed=19819847;
RA   Huang D., Li J., He L.Q.;
RT   "Influence of Tripterygium wilfordii on the expression of
RT   spermiogenesis related genes Herc4, Ipo11 and Mrto4 in mice.";
RL   Yi Chuan 31:941-946(2009).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase involved in either
CC       protein trafficking or in the distribution of cellular structures.
CC       Required for spermatozoon maturation and fertility, and for the
CC       removal of the cytoplasmic droplet of the spermatozoon. E3
CC       ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-
CC       conjugating enzyme in the form of a thioester and then directly
CC       transfer it to targeted substrates.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PAV2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PAV2-2; Sequence=VSP_023182;
CC       Name=3;
CC         IsoId=Q6PAV2-3; Sequence=VSP_023180, VSP_023181;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, highest expression is
CC       found in testis during spermiogenesis. It is specifically found in
CC       spermatogonia, spermatocytes, and spermatids with little or no
CC       expression detectable in the spermatozoa, or interstitial cells.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in testis during
CC       spermiogenesis. Expression was almost undetectable in testes at
CC       postnatal day 14 (P14). However, by P23, a strong increase in mRNA
CC       levels was observed with expression persisting to P40 when
CC       spermatozoa were first observed. Up-regulated in the uterine
CC       luminal epithelium at the time of embryo implantation.
CC   -!- DISRUPTION PHENOTYPE: Disruption causes defects in spermatozoon
CC       maturation and impaired fertility in males; females display normal
CC       fertility. Males produce litter sizes some 50% smaller, as well
CC       50% of mature spermatozoa have reduced mobility.
CC   -!- MISCELLANEOUS: T.wilfordii induces abnormal expression of
CC       spermiogenesis genes including Herc4, the spermatogenic cells in
CC       the convoluted seminiferous tubules decrease and the lumen is
CC       obstructed by large deciduous spermatogenic cells. T.wilfordii has
CC       apparent antifertility effects.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 7 RCC1 repeats.
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DR   EMBL; AK009436; BAB26286.1; -; mRNA.
DR   EMBL; AK143111; BAE25272.1; -; mRNA.
DR   EMBL; AK145735; BAE26617.1; -; mRNA.
DR   EMBL; AK147723; BAE28095.1; -; mRNA.
DR   EMBL; BC026855; AAH26855.1; -; mRNA.
DR   EMBL; BC043082; AAH43082.1; -; mRNA.
DR   EMBL; BC047157; AAH47157.1; -; mRNA.
DR   EMBL; BC060033; AAH60033.1; -; mRNA.
DR   RefSeq; NP_080377.2; NM_026101.4.
DR   RefSeq; NP_084390.1; NM_030114.2.
DR   UniGene; Mm.234437; -.
DR   UniGene; Mm.422789; -.
DR   UniGene; Mm.441725; -.
DR   UniGene; Mm.487274; -.
DR   ProteinModelPortal; Q6PAV2; -.
DR   SMR; Q6PAV2; 1-380, 655-1051.
DR   IntAct; Q6PAV2; 1.
DR   MINT; MINT-8174110; -.
DR   PhosphoSite; Q6PAV2; -.
DR   PaxDb; Q6PAV2; -.
DR   PRIDE; Q6PAV2; -.
DR   Ensembl; ENSMUST00000020258; ENSMUSP00000020258; ENSMUSG00000020064. [Q6PAV2-2]
DR   GeneID; 67345; -.
DR   KEGG; mmu:67345; -.
DR   UCSC; uc007fka.2; mouse. [Q6PAV2-3]
DR   UCSC; uc007fkc.2; mouse. [Q6PAV2-2]
DR   UCSC; uc007fkd.2; mouse. [Q6PAV2-1]
DR   CTD; 26091; -.
DR   MGI; MGI:1914595; Herc4.
DR   eggNOG; COG5021; -.
DR   GeneTree; ENSGT00740000115199; -.
DR   HOVERGEN; HBG050878; -.
DR   InParanoid; Q6PAV2; -.
DR   KO; K10615; -.
DR   OMA; DFFINKK; -.
DR   OrthoDB; EOG71VSRW; -.
DR   TreeFam; TF315189; -.
DR   UniPathway; UPA00143; -.
DR   NextBio; 324318; -.
DR   PRO; PR:Q6PAV2; -.
DR   Bgee; Q6PAV2; -.
DR   CleanEx; MM_HERC4; -.
DR   Genevestigator; Q6PAV2; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   Gene3D; 2.130.10.30; -; 1.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00415; RCC1; 7.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS00626; RCC1_2; 3.
DR   PROSITE; PS50012; RCC1_3; 7.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Cytoplasm; Differentiation;
KW   Ligase; Reference proteome; Repeat; Spermatogenesis;
KW   Ubl conjugation pathway.
FT   CHAIN         1   1057       Probable E3 ubiquitin-protein ligase
FT                                HERC4.
FT                                /FTId=PRO_0000278217.
FT   REPEAT        1     51       RCC1 1.
FT   REPEAT       52    101       RCC1 2.
FT   REPEAT      102    154       RCC1 3.
FT   REPEAT      156    207       RCC1 4.
FT   REPEAT      208    259       RCC1 5.
FT   REPEAT      261    311       RCC1 6.
FT   REPEAT      313    366       RCC1 7.
FT   DOMAIN      730   1057       HECT.
FT   ACT_SITE   1025   1025       Glycyl thioester intermediate (By
FT                                similarity).
FT   VAR_SEQ     229    233       DRYVP -> GRCAL (in isoform 3).
FT                                /FTId=VSP_023180.
FT   VAR_SEQ     234   1057       Missing (in isoform 3).
FT                                /FTId=VSP_023181.
FT   VAR_SEQ     643    650       Missing (in isoform 2).
FT                                /FTId=VSP_023182.
FT   CONFLICT    299    299       V -> A (in Ref. 2; AAH60033).
FT   CONFLICT    800    800       V -> I (in Ref. 1; BAE25272).
FT   CONFLICT    898    898       D -> N (in Ref. 1; BAE26617).
SQ   SEQUENCE   1057 AA;  118412 MW;  FCFFC9481AB0D4AE CRC64;
     MLCWGNASYG QLGLGGIDEE IVLEPRRSDF FVNKKVRDVG CGLRHTVFVL DDGTVYTCGC
     NDLGQLGHEK SRKKPEQVVA LDAQNIVAVA CGEAHTLALN DKGQVYAWGL DSDGQLGLQG
     SEECIRVPRN IKSLSDIQIV QVACGYYHSL ALSKASEVFC WGQNKYGQLG LGIDCQKQTS
     PQLIKSLLGI PFMQVAAGGA HSFVLTLSGA IFGWGRNKFG QLGLNDENDR YVPNLLKSLR
     SQKIVYICCG EDHTAALTKE GGVFTFGAGG YGQLGHNSTS HEINPRKVFE LMGSIVTQVA
     CGRQHTSAFV PSSGRIYSFG LGGNGQLGTG STSNRKSPFT VKGNWFSYNG QCPQDIGSED
     YFCVKRIFSG GDQSFSHYSS PQNCGPPDDF RCSDPSKQIW TVNEALIQKW LSYPSGRFPV
     EIANEIDGTF SSSGCLNGSF LAISNDDHYR TGTRFSGVDM NAARLLFHKL IQPDHPQISQ
     QVAASLEKNL IPKLTSSLPD VEALRFYLTL PECPLMSDCN NFTTIAIPFG TALVNLEKAP
     LKVLENWWSV LEPPLFLKIV ELFKEVVVHL LKLYKIGIPP SERRIFNSFL HTALKVLEIL
     HRVNEKTGQL IQYDKFYIHE VQELIDIRND YINWVQQQAY GVDVSHGVTE LADIPVTICT
     YPFVFDAQAK TTLLQTDAVL QMQMAIDQAH RQNVSSLFLP VIESVNPCLI LVVRRENIVG
     DAMEVLRKTK NIDYKKPLKV IFVGEDAVDA GGVRKEFFLL IMRELLDPKY GMFRYYEDSR
     LIWFSDKTFE DSDLFHLIGV ICGLAIYNFT IVDLHFPLAL YKKLLKRKPS LDDLKELMPA
     VGRSMQQLLD YPEDDIEETF CLNFTITVEN FGATEVKELV LNGADTAVNR QNRQEFVDAY
     VDYIFNKSVA SLFDAFHAGF HKVCGGKVLL LFQPNELQAM VIGNTNYDWK ELEKNTEYKG
     EYWADHPTIK IFWEVFHELP LEKKKQFLLF LTGSDRIPIL GMKSLKLVIQ STGGGESYLP
     VSHTCFNLLD LPKYTEKETL RCKLIQAIDH NEGFSLI
//
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