ID   RN103_HUMAN             Reviewed;         685 AA.
AC   O00237; A6NFV6; B2RAG4; Q53SU6; Q8IVB9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   02-DEC-2020, entry version 146.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF103;
DE            EC=2.3.2.27;
DE   AltName: Full=KF-1;
DE            Short=hKF-1;
DE   AltName: Full=RING finger protein 103;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF103 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 103 homolog;
DE            Short=Zfp-103;
GN   Name=RNF103; Synonyms=ZFP103;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9070305; DOI=10.1006/bbrc.1996.6033;
RA   Yasojima K., Tsujimura A., Mizuno T., Shigeyoshi Y., Inazawa J., Kikuno R.,
RA   Kuma K., Ohkubo K., Hosokawa Y., Ibata Y., Abe T., Miyata T., Matsubara K.,
RA   Nakajima K., Hashimoto-Gotoh T.;
RT   "Cloning of human and mouse cDNAs encoding novel zinc finger proteins
RT   expressed in cerebellum and hippocampus.";
RL   Biochem. Biophys. Res. Commun. 231:481-487(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Peripheral blood;
RA   Tsujimura A., Hashimoto-Gotoh T.;
RT   "Structure of human kf-1 genomic DNA.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [6]
RP   FUNCTION, AND MUTAGENESIS OF CYS-621.
RX   PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA   Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.;
RT   "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT   ubiquitination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DERL1 AND VCP.
RX   PubMed=18675248; DOI=10.1016/j.bbrc.2008.07.126;
RA   Maruyama Y., Yamada M., Takahashi K., Yamada M.;
RT   "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated
RT   degradation pathway.";
RL   Biochem. Biophys. Res. Commun. 374:737-741(2008).
CC   -!- FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably
CC       involved in the ER-associated protein degradation pathway.
CC       {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18675248}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DERL1 and VCP. {ECO:0000269|PubMed:18675248}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:18675248}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18675248}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the normal cerebellum but not
CC       in the cerebral cortex. {ECO:0000269|PubMed:9070305}.
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DR   EMBL; D76444; BAA19739.1; -; mRNA.
DR   EMBL; AB052743; BAB20900.1; -; Genomic_DNA.
DR   EMBL; AK314180; BAG36861.1; -; mRNA.
DR   EMBL; AC015971; AAX93079.1; -; Genomic_DNA.
DR   EMBL; BC035053; AAH35053.1; -; mRNA.
DR   EMBL; BC110333; AAI10334.1; -; mRNA.
DR   CCDS; CCDS33237.1; -.
DR   PIR; JC5392; JC5392.
DR   RefSeq; NP_001185880.1; NM_001198951.1.
DR   RefSeq; NP_001185881.1; NM_001198952.1.
DR   RefSeq; NP_005658.1; NM_005667.3.
DR   SMR; O00237; -.
DR   BioGRID; 113601; 14.
DR   IntAct; O00237; 10.
DR   STRING; 9606.ENSP00000237455; -.
DR   iPTMnet; O00237; -.
DR   PhosphoSitePlus; O00237; -.
DR   BioMuta; RNF103; -.
DR   jPOST; O00237; -.
DR   MassIVE; O00237; -.
DR   PaxDb; O00237; -.
DR   PeptideAtlas; O00237; -.
DR   PRIDE; O00237; -.
DR   ProteomicsDB; 47801; -.
DR   Antibodypedia; 34817; 122 antibodies.
DR   DNASU; 7844; -.
DR   Ensembl; ENST00000237455; ENSP00000237455; ENSG00000239305.
DR   GeneID; 7844; -.
DR   KEGG; hsa:7844; -.
DR   UCSC; uc002srn.4; human.
DR   CTD; 7844; -.
DR   DisGeNET; 7844; -.
DR   EuPathDB; HostDB:ENSG00000239305.6; -.
DR   GeneCards; RNF103; -.
DR   HGNC; HGNC:12859; RNF103.
DR   HPA; ENSG00000239305; Low tissue specificity.
DR   MIM; 602507; gene.
DR   neXtProt; NX_O00237; -.
DR   OpenTargets; ENSG00000239305; -.
DR   PharmGKB; PA37448; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00390000006413; -.
DR   HOGENOM; CLU_031351_0_0_1; -.
DR   InParanoid; O00237; -.
DR   OMA; TIYNSEH; -.
DR   OrthoDB; 1487241at2759; -.
DR   PhylomeDB; O00237; -.
DR   TreeFam; TF329229; -.
DR   PathwayCommons; O00237; -.
DR   Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 7844; 18 hits in 845 CRISPR screens.
DR   GenomeRNAi; 7844; -.
DR   Pharos; O00237; Tbio.
DR   PRO; PR:O00237; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O00237; protein.
DR   Bgee; ENSG00000239305; Expressed in middle temporal gyrus and 246 other tissues.
DR   Genevisible; O00237; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:Reactome.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR042494; RNF103.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15302; PTHR15302; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..685
FT                   /note="E3 ubiquitin-protein ligase RNF103"
FT                   /id="PRO_0000056084"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         621..663
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   MUTAGEN         621
FT                   /note="C->S: Loss of E2-dependent ubiquitination."
FT                   /evidence="ECO:0000269|PubMed:10500182"
FT   CONFLICT        22
FT                   /note="F -> L (in Ref. 3; BAG36861)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="S -> P (in Ref. 5; AAH35053)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="S -> P (in Ref. 3; BAG36861)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        502
FT                   /note="P -> H (in Ref. 5; AAH35053)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   685 AA;  79405 MW;  5AE7283EB38F533F CRC64;
     MWLKLFFLLL YFLVLFVLAR FFEAIVWYET GIFATQLVDP VALSFKKLKT ILECRGLGYS
     GLPEKKDVRE LVEKSGDLME GELYSALKEE EASESVSSTN FSGEMHFYEL VEDTKDGIWL
     VQVIANDRSP LVGKIHWEKM VKKVSRFGIR TGTFNCSSDP RYCRRRGWVR STLIMSVPQT
     STSKGKVMLK EYSGRKIEVE HIFKWITAHA ASRIKTIYNA EHLKEEWNKS DQYWLKIYLF
     ANLDQPPAFF SALSIKFTGR VEFIFVNVEN WDNKSYMTDI GIYNMPSYIL RTPEGIYRYG
     NHTGEFISLQ AMDSFLRSLQ PEVNDLFVLS LVLVNLMAWM DLFITQGATI KRFVVLISTL
     GTYNSLLIIS WLPVLGFLQL PYLDSFYEYS LKLLRYSNTT TLASWVRADW MFYSSHPALF
     LSTYLGHGLL IDYFEKKRRR NNNNDEVNAN NLEWLSSLWD WYTSYLFHPI ASFQNFPVES
     DWDEDPDLFL ERLAFPDLWL HPLIPTDYIK NLPMWRFKCL GVQSEEEMSE GSQDTENDSE
     SENTDTLSSE KEVFEDKQSV LHNSPGTASH CDAEACSCAN KYCQTSPCER KGRSYGSYNT
     NEDMEPDWLT WPADMLHCTE CVVCLENFEN GCLLMGLPCG HVFHQNCIVM WLAGGRHCCP
     VCRWPSYKKK QPYAQHQPLS NDVPS
//