ZFPL1_MOUSE
ID ZFPL1_MOUSE Reviewed; 310 AA.
AC Q9DB43;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Zinc finger protein-like 1;
GN Name=Zfpl1;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, Spleen, and 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: Required for cis-Golgi integrity and efficient ER to Golgi
CC transport. Involved in the maintenance of the integrity of the cis-
CC Golgi, possibly via its interaction with GOLGA2/GM130 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GOLGA2/GM130. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9DB43; Q62839: Golga2; Xeno; NbExp=14; IntAct=EBI-7836139, EBI-618335;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The B box-type and RING-type zinc fingers although degenerate
CC play a central role in function of the protein. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZFPL1 family. {ECO:0000305}.
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DR EMBL; AK005244; BAB23901.1; -; mRNA.
DR EMBL; BC002119; AAH02119.1; -; mRNA.
DR CCDS; CCDS29492.1; -.
DR RefSeq; NP_077193.1; NM_024231.2.
DR RefSeq; XP_006531924.1; XM_006531861.1.
DR RefSeq; XP_006531925.1; XM_006531862.1.
DR RefSeq; XP_006531926.1; XM_006531863.3.
DR AlphaFoldDB; Q9DB43; -.
DR BioGRID; 219904; 4.
DR IntAct; Q9DB43; 1.
DR MINT; Q9DB43; -.
DR STRING; 10090.ENSMUSP00000025707; -.
DR iPTMnet; Q9DB43; -.
DR PhosphoSitePlus; Q9DB43; -.
DR EPD; Q9DB43; -.
DR MaxQB; Q9DB43; -.
DR PaxDb; Q9DB43; -.
DR PeptideAtlas; Q9DB43; -.
DR PRIDE; Q9DB43; -.
DR ProteomicsDB; 275062; -.
DR Antibodypedia; 2657; 109 antibodies from 20 providers.
DR DNASU; 81909; -.
DR Ensembl; ENSMUST00000025707; ENSMUSP00000025707; ENSMUSG00000024792.
DR GeneID; 81909; -.
DR KEGG; mmu:81909; -.
DR UCSC; uc008ghg.1; mouse.
DR CTD; 7542; -.
DR MGI; MGI:1891017; Zfpl1.
DR VEuPathDB; HostDB:ENSMUSG00000024792; -.
DR eggNOG; KOG3970; Eukaryota.
DR GeneTree; ENSGT00390000009753; -.
DR InParanoid; Q9DB43; -.
DR OMA; PNCALCN; -.
DR OrthoDB; 807302at2759; -.
DR PhylomeDB; Q9DB43; -.
DR TreeFam; TF315090; -.
DR BioGRID-ORCS; 81909; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zfpl1; mouse.
DR PRO; PR:Q9DB43; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9DB43; protein.
DR Bgee; ENSMUSG00000024792; Expressed in yolk sac and 222 other tissues.
DR ExpressionAtlas; Q9DB43; baseline and differential.
DR Genevisible; Q9DB43; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR039043; ZFPL1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12981; PTHR12981; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW ER-Golgi transport; Golgi apparatus; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..310
FT /note="Zinc finger protein-like 1"
FT /id="PRO_0000056319"
FT TOPO_DOM 1..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..310
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ZN_FING 1..43
FT /note="B box-type; degenerate"
FT ZN_FING 53..101
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 162..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 310 AA; 34155 MW; 55BF8A67B26B4B94 CRC64;
MGLCKCPKRK VTNLFCFEHR VNVCEHCLVA NHAKCIVQSY LQWLQDSDYN PNCRLCNTPL
ASRETTRLVC YDLFHWACIN ERAAQLPRNT APAGYQCPSC NGPIFPPANL AGPVASALRE
KLATVNWARA GLGLPLIDEV ISPEPEPLNS SDFSDWSSFN ATTTSVQEER ASTPSAPAFY
SQAPRPPPSP SRPEQHTVIH MGSTEALAHA PRKVYDTRDD DRTAGIHGDC DDDKYRRRPA
LGWLAQLLRS RAGSRKRPLT LLQRAGLLLL LGLLGFLALL ALMSRLGRAA ADSDPNLDPL
MNPHIRVGPS
