CCZ1_HUMAN
ID CCZ1_HUMAN Reviewed; 482 AA.
AC P86791; A2RU45; O95766; Q9UG65; Q9Y359;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Vacuolar fusion protein CCZ1 homolog;
GN Name=CCZ1; Synonyms=C7orf28A; ORFNames=CGI-43;
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].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, AND INTERACTION WITH MON1A.
RX PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
RA Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
RT "BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
RT nucleotide exchange factor.";
RL Curr. Biol. 22:2135-2139(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH RMC1; CCZ1; MON1A AND MON1B.
RX PubMed=29038162; DOI=10.1128/mcb.00392-17;
RA Pontano Vaites L., Paulo J.A., Huttlin E.L., Harper J.W.;
RT "Systematic analysis of human cells lacking ATG8 proteins uncovers roles
RT for GABARAPs and the CCZ1/MON1 regulator C18orf8/RMC1 in macro and
RT selective autophagic flux.";
RL Mol. Cell. Biol. 0:0-0(2017).
CC -!- FUNCTION: Acts in concert with MON1A, as a guanine exchange factor
CC (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from
CC an inactive GDP-bound form into an active GTP-bound form
CC (PubMed:23084991). {ECO:0000269|PubMed:23084991}.
CC -!- SUBUNIT: Interacts with MON1A (PubMed:23084991). Found in a complex
CC with RMC1, CCZ1, MON1A and MON1B (PubMed:29038162).
CC {ECO:0000269|PubMed:23084991, ECO:0000269|PubMed:29038162}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319}.
CC -!- SIMILARITY: Belongs to the CCZ1 family. {ECO:0000305}.
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DR EMBL; AF151801; AAD34038.1; -; mRNA.
DR EMBL; AK292326; BAF85015.1; -; mRNA.
DR EMBL; AC004983; AAQ96868.1; -; Genomic_DNA.
DR EMBL; BC132749; AAI32750.1; -; mRNA.
DR EMBL; BC132751; AAI32752.1; -; mRNA.
DR CCDS; CCDS34597.1; -.
DR PIR; T08806; T08806.
DR RefSeq; NP_056437.4; NM_015622.5.
DR RefSeq; NP_932765.1; NM_198097.3.
DR AlphaFoldDB; P86791; -.
DR SMR; P86791; -.
DR BioGRID; 119643; 81.
DR BioGRID; 128773; 7.
DR iPTMnet; P86791; -.
DR PhosphoSitePlus; P86791; -.
DR BioMuta; CCZ1; -.
DR DMDM; 310943082; -.
DR EPD; P86791; -.
DR jPOST; P86791; -.
DR MassIVE; P86791; -.
DR MaxQB; P86791; -.
DR PRIDE; P86791; -.
DR Antibodypedia; 57705; 128 antibodies from 21 providers.
DR DNASU; 51622; -.
DR Ensembl; ENST00000325974.9; ENSP00000325681.6; ENSG00000122674.12.
DR GeneID; 221960; -.
DR GeneID; 51622; -.
DR KEGG; hsa:221960; -.
DR KEGG; hsa:51622; -.
DR MANE-Select; ENST00000316731.13; ENSP00000314544.8; NM_198097.5; NP_932765.1.
DR MANE-Select; ENST00000325974.9; ENSP00000325681.6; NM_015622.6; NP_056437.4.
DR UCSC; uc003spf.4; human.
DR CTD; 221960; -.
DR CTD; 51622; -.
DR DisGeNET; 221960; -.
DR DisGeNET; 51622; -.
DR GeneCards; CCZ1; -.
DR HGNC; HGNC:21691; CCZ1.
DR HPA; ENSG00000122674; Low tissue specificity.
DR neXtProt; NX_P86791; -.
DR OpenTargets; ENSG00000122674; -.
DR VEuPathDB; HostDB:ENSG00000122674; -.
DR GeneTree; ENSGT00390000004713; -.
DR HOGENOM; CLU_037828_2_0_1; -.
DR InParanoid; P86791; -.
DR OMA; FLRAQNF; -.
DR OrthoDB; 448107at2759; -.
DR PhylomeDB; P86791; -.
DR TreeFam; TF314962; -.
DR PathwayCommons; P86791; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P86791; -.
DR BioGRID-ORCS; 221960; 41 hits in 960 CRISPR screens.
DR BioGRID-ORCS; 51622; 20 hits in 313 CRISPR screens.
DR ChiTaRS; CCZ1; human.
DR Pharos; P86791; Tbio.
DR PRO; PR:P86791; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P86791; protein.
DR Bgee; ENSG00000122674; Expressed in mucosa of transverse colon and 96 other tissues.
DR ExpressionAtlas; P86791; baseline and differential.
DR Genevisible; P86791; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR013176; Ccz1.
DR InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR InterPro; IPR043989; CCZ1/INTU/HSP4_longin_3.
DR InterPro; IPR043988; CCZ1/INTU_longin_2.
DR PANTHER; PTHR13056; PTHR13056; 1.
DR Pfam; PF19031; Intu_longin_1; 1.
DR Pfam; PF19032; Intu_longin_2; 1.
DR Pfam; PF19033; Intu_longin_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Guanine-nucleotide releasing factor; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..482
FT /note="Vacuolar fusion protein CCZ1 homolog"
FT /id="PRO_0000401065"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT CONFLICT 5..15
FT /note="AAGAGSGPWAA -> QRRPGPGAGLGG (in Ref. 1; AAD34038)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="N -> C (in Ref. 1; AAD34038)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..162
FT /note="LKAMEDGGVK -> PESHGRRRVQ (in Ref. 1; AAD34038)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..449
FT /note="EL -> DS (in Ref. 1; AAD34038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 55866 MW; EE10E55EEC918C18 CRC64;
MAAAAAGAGS GPWAAQEKQF PPALLSFFIY NPRFGPREGQ EENKILFYHP NEVEKNEKIR
NVGLCEAIVQ FTRTFSPSKP AKSLHTQKNR QFFNEPEENF WMVMVVRNPI IEKQSKDGKP
VIEYQEEELL DKVYSSVLRQ CYSMYKLFNG TFLKAMEDGG VKLLKERLEK FFHRYLQTLH
LQSCDLLDIF GGISFFPLDK MTYLKIQSFI NRMEESLNIV KYTAFLYNDQ LIWSGLEQDD
MRILYKYLTT SLFPRHIEPE LAGRDSPIRA EMPGNLQHYG RFLTGPLNLN DPDAKCRFPK
IFVNTDDTYE ELHLIVYKAM SAAVCFMIDA SVHPTLDFCR RLDSIVGPQL TVLASDICEQ
FNINKRMSGS EKEPQFKFIY FNHMNLAEKS TVHMRKTPSV SLTSVHPDLM KILGDINSDF
TRVDEDEEII VKAMSDYWVV GKKSDRRELY VILNQKNANL IEVNEEVKKL CATQFNNIFF
LD
