YIPF5_MOUSE
ID YIPF5_MOUSE Reviewed; 257 AA.
AC Q9EQQ2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein YIPF5 {ECO:0000305};
DE AltName: Full=YIP1 family member 5;
DE AltName: Full=YPT-interacting protein 1 A;
GN Name=Yipf5 {ECO:0000312|MGI:MGI:1914430}; Synonyms=Yip1a;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11489904; DOI=10.1074/jbc.m106189200;
RA Tang B.L., Ong Y.S., Huang B., Wei S., Wong E.T., Qi R., Horstmann H.,
RA Hong W.;
RT "A membrane protein enriched in endoplasmic reticulum exit sites interacts
RT with COPII.";
RL J. Biol. Chem. 276:40008-40017(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Placenta, and Tongue;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Eye, and Mammary tumor;
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 SUBCELLULAR LOCATION.
RX PubMed=15254263; DOI=10.1091/mbc.e03-11-0822;
RA Kano F., Tanaka A.R., Yamauchi S., Kondo H., Murata M.;
RT "Cdc2 kinase-dependent disassembly of endoplasmic reticulum (ER) exit sites
RT inhibits ER-to-Golgi vesicular transport during mitosis.";
RL Mol. Biol. Cell 15:4289-4298(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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: Plays a role in transport between endoplasmic reticulum and
CC Golgi. In pancreatic beta cells, required to transport proinsulin from
CC endoplasmic reticulum into the Golgi. {ECO:0000250|UniProtKB:Q969M3}.
CC -!- SUBUNIT: Interacts with the COPII coat components Sec23 (SEC23A and/or
CC SEC23B) and Sec24 (SEC24A and/or SEC24B) (By similarity). Interacts
CC with YIF1A (By similarity). May interact with RAB1A (By similarity).
CC Interacts with YIPF3 and YIPF4 (By similarity).
CC {ECO:0000250|UniProtKB:Q969M3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:15254263}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15254263}. Cytoplasmic vesicle, COPII-coated
CC vesicle {ECO:0000250|UniProtKB:Q5XID0}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15254263}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15254263}. Note=Enriched at the endoplasmic
CC reticulum exit sites (PubMed:15254263). Incorporated into COPII coated
CC vesicles (By similarity). {ECO:0000250|UniProtKB:Q5XID0,
CC ECO:0000269|PubMed:15254263}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11489904}.
CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR EMBL; AF140226; AAG48522.1; -; mRNA.
DR EMBL; AK010089; BAB26694.1; -; mRNA.
DR EMBL; AK151425; BAE30389.1; -; mRNA.
DR EMBL; AK151461; BAE30419.1; -; mRNA.
DR EMBL; AK152440; BAE31221.1; -; mRNA.
DR EMBL; AK153123; BAE31738.1; -; mRNA.
DR EMBL; AK160004; BAE35552.1; -; mRNA.
DR EMBL; AK167526; BAE39596.1; -; mRNA.
DR EMBL; BC003317; AAH03317.1; -; mRNA.
DR EMBL; BC055301; AAH55301.1; -; mRNA.
DR CCDS; CCDS29207.1; -.
DR RefSeq; NP_075800.1; NM_023311.3.
DR AlphaFoldDB; Q9EQQ2; -.
DR BioGRID; 211998; 2.
DR STRING; 10090.ENSMUSP00000025364; -.
DR iPTMnet; Q9EQQ2; -.
DR PhosphoSitePlus; Q9EQQ2; -.
DR EPD; Q9EQQ2; -.
DR MaxQB; Q9EQQ2; -.
DR PaxDb; Q9EQQ2; -.
DR PeptideAtlas; Q9EQQ2; -.
DR PRIDE; Q9EQQ2; -.
DR ProteomicsDB; 299629; -.
DR Antibodypedia; 45624; 121 antibodies from 21 providers.
DR DNASU; 67180; -.
DR Ensembl; ENSMUST00000025364; ENSMUSP00000025364; ENSMUSG00000024487.
DR GeneID; 67180; -.
DR KEGG; mmu:67180; -.
DR UCSC; uc008etd.1; mouse.
DR CTD; 81555; -.
DR MGI; MGI:1914430; Yipf5.
DR VEuPathDB; HostDB:ENSMUSG00000024487; -.
DR eggNOG; KOG3103; Eukaryota.
DR GeneTree; ENSGT00940000153168; -.
DR HOGENOM; CLU_074741_2_0_1; -.
DR InParanoid; Q9EQQ2; -.
DR OMA; IGINFDH; -.
DR OrthoDB; 1457080at2759; -.
DR PhylomeDB; Q9EQQ2; -.
DR TreeFam; TF313100; -.
DR BioGRID-ORCS; 67180; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Yipf5; mouse.
DR PRO; PR:Q9EQQ2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9EQQ2; protein.
DR Bgee; ENSMUSG00000024487; Expressed in lacrimal gland and 263 other tissues.
DR Genevisible; Q9EQQ2; MM.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0030070; P:insulin processing; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:MGI.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR InterPro; IPR045231; Yip1/4-like.
DR PANTHER; PTHR21236; PTHR21236; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..257
FT /note="Protein YIPF5"
FT /id="PRO_0000234330"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q969M3"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..196
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 75..106
FT /note="Interaction with Sec23"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 27873 MW; 792206E7E4B39190 CRC64;
MSGFDNLNSG FYQTSYSIDE QSQQSYDYGG SGGPYSKQYA GCDYSQQGRF VPPDMMQPQQ
TYTGQIYQPT QAYPPTTPQP FYGDSFEEEP PLLEELGINF DHIWQKTLTV LHPLRAADGS
IMNETDLAGP VVFCLAFGAT LLLAGKIQFG YVYGISAIGC LGMFCLLNLM SMTGVSFGCV
ASVLGYCLLP MILLSSFAVV FSLQGMVGIL LTATIIGWCS FSASKIFISA LAMDGQQLLV
AYPCALLYGV FALISVF
