TMCC1_MOUSE
ID TMCC1_MOUSE Reviewed; 649 AA.
AC Q69ZZ6; Q8CEF4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transmembrane and coiled-coil domains protein 1 {ECO:0000250|UniProtKB:O94876};
GN Name=Tmcc1; Synonyms=Kiaa0779 {ECO:0000303|PubMed:15368895};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Endoplasmic reticulum membrane protein that promotes
CC endoplasmic reticulum-associated endosome fission. Localizes to contact
CC sites between the endoplasmic reticulum and endosomes and acts by
CC promoting recruitment of the endoplasmic reticulum to endosome tubules
CC for fission. Endosome membrane fission of early and late endosomes is
CC essential to separate regions destined for lysosomal degradation from
CC carriers to be recycled to the plasma membrane.
CC {ECO:0000250|UniProtKB:O94876}.
CC -!- SUBUNIT: May form homodimers and heterodimers with TMCC2 or TMCC3 via
CC the coiled-coil domains. Interacts with ribosomal proteins RPL4 and
CC RPS6. {ECO:0000250|UniProtKB:O94876}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O94876}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Specifically localizes to contact sites between the
CC endoplasmic reticulum and endosomes that are spatially and temporally
CC linked to endosome fission. {ECO:0000250|UniProtKB:O94876}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q69ZZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZZ6-2; Sequence=VSP_019590, VSP_019591;
CC Name=3;
CC IsoId=Q69ZZ6-3; Sequence=VSP_019589;
CC -!- SIMILARITY: Belongs to the TEX28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE32665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173022; BAD32300.1; ALT_INIT; mRNA.
DR EMBL; AK028322; BAC25880.1; -; mRNA.
DR EMBL; AK154540; BAE32665.1; ALT_INIT; mRNA.
DR CCDS; CCDS51881.1; -. [Q69ZZ6-1]
DR CCDS; CCDS90105.1; -. [Q69ZZ6-3]
DR RefSeq; NP_803131.1; NM_177412.1. [Q69ZZ6-1]
DR RefSeq; XP_006506371.1; XM_006506308.2. [Q69ZZ6-1]
DR RefSeq; XP_006506373.1; XM_006506310.1. [Q69ZZ6-2]
DR RefSeq; XP_006506377.1; XM_006506314.3.
DR RefSeq; XP_017177146.1; XM_017321657.1. [Q69ZZ6-3]
DR AlphaFoldDB; Q69ZZ6; -.
DR SMR; Q69ZZ6; -.
DR STRING; 10090.ENSMUSP00000086285; -.
DR iPTMnet; Q69ZZ6; -.
DR PhosphoSitePlus; Q69ZZ6; -.
DR jPOST; Q69ZZ6; -.
DR MaxQB; Q69ZZ6; -.
DR PaxDb; Q69ZZ6; -.
DR PRIDE; Q69ZZ6; -.
DR ProteomicsDB; 259569; -. [Q69ZZ6-1]
DR ProteomicsDB; 259570; -. [Q69ZZ6-2]
DR ProteomicsDB; 259571; -. [Q69ZZ6-3]
DR Antibodypedia; 33295; 114 antibodies from 19 providers.
DR Ensembl; ENSMUST00000088896; ENSMUSP00000086285; ENSMUSG00000030126. [Q69ZZ6-1]
DR Ensembl; ENSMUST00000172510; ENSMUSP00000133665; ENSMUSG00000030126. [Q69ZZ6-3]
DR Ensembl; ENSMUST00000173140; ENSMUSP00000134455; ENSMUSG00000030126. [Q69ZZ6-3]
DR Ensembl; ENSMUST00000204353; ENSMUSP00000144971; ENSMUSG00000030126. [Q69ZZ6-2]
DR GeneID; 330401; -.
DR KEGG; mmu:330401; -.
DR UCSC; uc009djo.2; mouse. [Q69ZZ6-1]
DR UCSC; uc009djp.2; mouse. [Q69ZZ6-2]
DR CTD; 23023; -.
DR MGI; MGI:2442368; Tmcc1.
DR VEuPathDB; HostDB:ENSMUSG00000030126; -.
DR eggNOG; KOG3850; Eukaryota.
DR GeneTree; ENSGT00940000155189; -.
DR InParanoid; Q69ZZ6; -.
DR OMA; QADMEPE; -.
DR OrthoDB; 1175041at2759; -.
DR PhylomeDB; Q69ZZ6; -.
DR TreeFam; TF316292; -.
DR BioGRID-ORCS; 330401; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tmcc1; mouse.
DR PRO; PR:Q69ZZ6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q69ZZ6; protein.
DR Bgee; ENSMUSG00000030126; Expressed in granulocyte and 231 other tissues.
DR ExpressionAtlas; Q69ZZ6; baseline and differential.
DR Genevisible; Q69ZZ6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0140285; P:endosome fission; ISS:UniProtKB.
DR GO; GO:0097750; P:endosome membrane tubulation; ISS:UniProtKB.
DR GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR InterPro; IPR019394; TEX28/TMCC.
DR PANTHER; PTHR17613; PTHR17613; 1.
DR Pfam; PF10267; Tmemb_cc2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="Transmembrane and coiled-coil domains protein 1"
FT /id="PRO_0000184596"
FT TOPO_DOM 1..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..310
FT /evidence="ECO:0000255"
FT COILED 457..566
FT /evidence="ECO:0000255"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O94876"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..320
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019589"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019590"
FT VAR_SEQ 176..188
FT /note="GVCVPGEEATAER -> MVQRFSLRRQLSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019591"
SQ SEQUENCE 649 AA; 71642 MW; 6A7E07076CD3BF08 CRC64;
MEPSGSEQLY EDPDPGGKSQ DAEARRQTES EQKLSKMTHN ALENINVIGQ GLKHLFQHQR
RRSSVSPHDV QQIQTDPEPE VDLDSQNACA EIDGVSTHPT ALNRVLQQIR VPPKMKRGTS
LHSRRGKSEA PKGSPQINRK SGQEVAAVIQ SGRPRSSSTT DAPTSSSVME IACAAGVCVP
GEEATAERIE RLEVSSLAQT SSAVASSTDG SIHTESVDGI PDPQRTKAAI AHLQQKILKL
TEQIKIAQTA RDDNVAEYLK LANSADKQQA ARIKQVFEKK NQKSAQTILQ LQKKLEHYHR
KLREVEQNGI PRQPKDVFRD MHQGLKDVGA KVTGFSEGVV DSVKGGFSSF SQATHSAAGA
VVSKPREIAS LIRNKFGSAD NIPNLKDSLE EGQVDDGGKA LGVISNFQSS PKYGSEEDCS
SATSGSVGAN STTGGIAVGA SSSKTNTLDM QSSGFDALLH EVQEIRETQA RLEDSFETLK
EHYQRDYSLI MQTLQEERYR CERLEEQLND LTELHQNEIL NLKQELASME EKIAYQSYER
ARDIQEALEA CQTRISKMEL QQQQQQVVQL EGLENATARN LLGKLINILL AVMAVLLVFV
STVANCVVPL MKTRNRTFST LFLVAFIAFL WKHWDALFSY VDRLFSPPR
