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ARMD3_HUMAN
ID   ARMD3_HUMAN             Reviewed;         689 AA.
AC   Q5T2E6; Q2TB87; Q9H8Z9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Armadillo-like helical domain-containing protein 3 {ECO:0000305};
GN   Name=ARMH3 {ECO:0000312|HGNC:HGNC:25788};
GN   Synonyms=C10orf76 {ECO:0000312|HGNC:HGNC:25788};
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 [LARGE SCALE MRNA] (ISOFORM 2).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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   INTERACTION WITH PI4KB.
RX   PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA   Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT   "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT   by enteroviral and kobuviral 3A protein binding.";
RL   MBio 4:E00098-E00098(2013).
RN   [5]
RP   SUBCELLULAR LOCATION, INTERACTION WITH GBF1, FUNCTION, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=31519766; DOI=10.1074/mcp.ra119.001645;
RA   Chan C.J., Le R., Burns K., Ahmed K., Coyaud E., Laurent E.M.N., Raught B.,
RA   Melancon P.;
RT   "BioID performed on Golgi enriched fractions identify C10orf76 as aGBF1
RT   Binding Protein essential for Golgi maintenance and secretion.";
RL   Mol. Cell. Proteomics 18:2285-2297(2019).
CC   -!- FUNCTION: Involved in GBF1 recruitment, Golgi maintenance and protein
CC       secretion. {ECO:0000269|PubMed:31519766}.
CC   -!- SUBUNIT: Interacts with PI4KB (PubMed:23572552). Interacts with GBF1
CC       (PubMed:31519766). {ECO:0000269|PubMed:23572552,
CC       ECO:0000269|PubMed:31519766}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:31519766}; Single-pass membrane protein
CC       {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:31519766}. Note=The
CC       majority of ARMD3 is cytosolic, with a portion colocalizing with GBF1
CC       at juxtanuclear Golgi sites. {ECO:0000269|PubMed:31519766}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5T2E6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5T2E6-2; Sequence=VSP_024552;
CC       Name=3;
CC         IsoId=Q5T2E6-3; Sequence=VSP_024552, VSP_024553, VSP_024554;
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ARMH3 family. {ECO:0000305}.
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DR   EMBL; AK023176; BAB14447.1; -; mRNA.
DR   EMBL; AC010789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC110511; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS41563.1; -. [Q5T2E6-1]
DR   RefSeq; NP_078817.2; NM_024541.2. [Q5T2E6-1]
DR   RefSeq; XP_011538453.1; XM_011540151.2. [Q5T2E6-1]
DR   AlphaFoldDB; Q5T2E6; -.
DR   BioGRID; 122733; 27.
DR   IntAct; Q5T2E6; 2.
DR   STRING; 9606.ENSP00000359050; -.
DR   iPTMnet; Q5T2E6; -.
DR   PhosphoSitePlus; Q5T2E6; -.
DR   BioMuta; C10orf76; -.
DR   DMDM; 74744614; -.
DR   EPD; Q5T2E6; -.
DR   jPOST; Q5T2E6; -.
DR   MassIVE; Q5T2E6; -.
DR   MaxQB; Q5T2E6; -.
DR   PaxDb; Q5T2E6; -.
DR   PeptideAtlas; Q5T2E6; -.
DR   PRIDE; Q5T2E6; -.
DR   ProteomicsDB; 64333; -. [Q5T2E6-1]
DR   ProteomicsDB; 64334; -. [Q5T2E6-2]
DR   ProteomicsDB; 64335; -. [Q5T2E6-3]
DR   Antibodypedia; 64513; 13 antibodies from 7 providers.
DR   DNASU; 79591; -.
DR   Ensembl; ENST00000370033.9; ENSP00000359050.4; ENSG00000120029.13. [Q5T2E6-1]
DR   GeneID; 79591; -.
DR   KEGG; hsa:79591; -.
DR   MANE-Select; ENST00000370033.9; ENSP00000359050.4; NM_024541.3; NP_078817.2.
DR   UCSC; uc009xwy.2; human. [Q5T2E6-1]
DR   CTD; 79591; -.
DR   DisGeNET; 79591; -.
DR   GeneCards; ARMH3; -.
DR   HGNC; HGNC:25788; ARMH3.
DR   HPA; ENSG00000120029; Low tissue specificity.
DR   neXtProt; NX_Q5T2E6; -.
DR   OpenTargets; ENSG00000120029; -.
DR   PharmGKB; PA134903060; -.
DR   VEuPathDB; HostDB:ENSG00000120029; -.
DR   eggNOG; KOG4654; Eukaryota.
DR   GeneTree; ENSGT00390000002554; -.
DR   HOGENOM; CLU_029861_2_0_1; -.
DR   InParanoid; Q5T2E6; -.
DR   OMA; GFWTEFF; -.
DR   PhylomeDB; Q5T2E6; -.
DR   TreeFam; TF300220; -.
DR   PathwayCommons; Q5T2E6; -.
DR   SignaLink; Q5T2E6; -.
DR   BioGRID-ORCS; 79591; 52 hits in 1065 CRISPR screens.
DR   ChiTaRS; ARMH3; human.
DR   GenomeRNAi; 79591; -.
DR   Pharos; Q5T2E6; Tdark.
DR   PRO; PR:Q5T2E6; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q5T2E6; protein.
DR   Bgee; ENSG00000120029; Expressed in left ventricle myocardium and 186 other tissues.
DR   ExpressionAtlas; Q5T2E6; baseline and differential.
DR   Genevisible; Q5T2E6; HS.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:1903358; P:regulation of Golgi organization; IMP:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039868; ARMD3-like.
DR   InterPro; IPR013636; ARMH3_C.
DR   PANTHER; PTHR13608; PTHR13608; 1.
DR   Pfam; PF08427; DUF1741; 1.
DR   SMART; SM01158; DUF1741; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Golgi apparatus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..689
FT                   /note="Armadillo-like helical domain-containing protein 3"
FT                   /id="PRO_0000284515"
FT   TRANSMEM        520..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..424
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024552"
FT   VAR_SEQ         569..584
FT                   /note="VLRLSTNAGQWKEAAS -> EPSSTTLTPKLSPTLL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024553"
FT   VAR_SEQ         585..689
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024554"
FT   CONFLICT        672
FT                   /note="A -> V (in Ref. 1; BAB14447)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   689 AA;  78710 MW;  5C21E860F3E2BD68 CRC64;
     MAQVEKRGGL LRKSSASKKP LKEKVVLMYD EIFMTEDPSK CSPRFWEELF LMKVNLEYLE
     GKLESLDGEE LMKIKDNINC LFQHCIQALG EEHPIRVVNA LQTLCALIRG VHQKNKSTSG
     FDIINMLMGF DKAELCMKNL MESLDSLLCA EGSESLKSLC LKLLLCLVTV TDNISQNTIL
     EYVMINSIFE AILQILSHPP SRREHGYDAV VLLALLVNYR KYESVNPYIV KLSIVDDEAT
     LNGMGLVIAQ ALSEYNRQYK DKEEEHQSGF FSALTNMVGS MFIADAHEKI SVQTNEAILL
     ALYEAVHLNR NFITVLAQSH PEMGLVTTPV SPAPTTPVTP LGTTPPSSDV ISSVELPLDA
     DVQTSNLLIT FLKYSSIVMQ DTKDEHRLHS GKLCLIILTC IAEDQYANAF LHDDNMNFRV
     NLHRMPMRHR KKAADKNLPC RPLVCAVLDL MVEFIVTHMM KEFPMDLYIR CIQVVHKLLC
     YQKKCRVRLH YTWRELWSAL INLLKFLMSN ETVLLAKHNI FTLALMIVNL FNMFITYGDT
     FLPTPSSYDE LYYEIIRMHQ SFDNLYSMVL RLSTNAGQWK EAASKVTHAL VNIRAIINHF
     NPKIESYAAV NHISQLSEEQ VLEVVRANYD TLTLKLQDGL DQYERYSEQH KEAAFFKELV
     RSISTNVRRN LAFHTLSQEV LLKEFSTIS
 
 
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