ID YIPF5_HUMAN Reviewed; 257 AA. AC Q969M3; D3DQF5; Q4VSN6; Q53EX4; Q8NHE5; Q9H338; Q9H3U4; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Protein YIPF5; DE AltName: Full=Five-pass transmembrane protein localizing in the Golgi apparatus and the endoplasmic reticulum 5; DE AltName: Full=Smooth muscle cell-associated protein 5; DE Short=SMAP-5; DE AltName: Full=YIP1 family member 5; DE AltName: Full=YPT-interacting protein 1 A; GN Name=YIPF5 {ECO:0000312|HGNC:HGNC:24877}; Synonyms=FINGER5, YIP1A; GN ORFNames=PP12723, SB140, UNQ3123/PRO10275; 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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SEC23 RP AND SEC24, AND SUBCELLULAR LOCATION. 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 [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND RP INDUCTION. RC TISSUE=Coronary artery; RX PubMed=15922870; DOI=10.1016/j.gene.2005.03.012; RA Stolle K., Schnoor M., Fuellen G., Spitzer M., Engel T., Spener F., RA Cullen P., Lorkowski S.; RT "Cloning, cellular localization, genomic organization, and tissue-specific RT expression of the TGFbeta1-inducible SMAP-5 gene."; RL Gene 351:119-130(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Zhang W., Li N., Zhang M., Wan T., Cao X.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Neuroblastoma; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney epithelium; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix, Eye, and Uterus; 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 [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 181-257 (ISOFORMS 1/2). RC TISSUE=Heart; RA Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.; RT "Molecular cloning and characterization of the human smooth muscle cell RT associated protein-5 (SMAP-5)."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [12] RP FUNCTION, AND INTERACTION WITH RAB1A. RX PubMed=15611160; DOI=10.1534/genetics.104.032888; RA Chen C.Z., Calero M., DeRegis C.J., Heidtman M., Barlowe C., Collins R.N.; RT "Genetic analysis of yeast Yip1p function reveals a requirement for Golgi- RT localized rab proteins and rab-Guanine nucleotide dissociation inhibitor."; RL Genetics 168:1827-1841(2004). RN [13] RP INTERACTION WITH YIF1A, AND SUBCELLULAR LOCATION. RX PubMed=15990086; DOI=10.1016/j.bbrc.2005.06.051; RA Jin C., Zhang Y., Zhu H., Ahmed K., Fu C., Yao X.; RT "Human Yip1A specifies the localization of Yif1 to the Golgi apparatus."; RL Biochem. Biophys. Res. Commun. 334:16-22(2005). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH YIPF3 AND YIPF4. RX PubMed=27999994; DOI=10.1007/s00418-016-1527-3; RA Kranjc T., Dempsey E., Cagney G., Nakamura N., Shields D.C., Simpson J.C.; RT "Functional characterisation of the YIPF protein family in mammalian RT cells."; RL Histochem. Cell Biol. 147:439-451(2017). RN [18] RP VARIANTS MEDS2 VAL-97; SER-98; LYS-106 DEL; VAL-181 AND ARG-218, RP CHARACTERIZATION OF VARIANT MEDS2 SER-98, TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, AND FUNCTION. RX PubMed=33164986; DOI=10.1172/jci141455; RA De Franco E., Lytrivi M., Ibrahim H., Montaser H., Wakeling M.N., RA Fantuzzi F., Patel K., Demarez C., Cai Y., Igoillo-Esteve M., Cosentino C., RA Lithovius V., Vihinen H., Jokitalo E., Laver T.W., Johnson M.B., RA Sawatani T., Shakeri H., Pachera N., Haliloglu B., Ozbek M.N., Unal E., RA Yildirim R., Godbole T., Yildiz M., Aydin B., Bilheu A., Suzuki I., RA Flanagan S.E., Vanderhaeghen P., Senee V., Julier C., Marchetti P., RA Eizirik D.L., Ellard S., Saarimaeki-Vire J., Otonkoski T., Cnop M., RA Hattersley A.T.; RT "YIPF5 mutations cause neonatal diabetes and microcephaly through RT endoplasmic reticulum stress."; RL J. Clin. Invest. 130:6338-6353(2020). 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 (PubMed:33164986). CC {ECO:0000269|PubMed:11489904, ECO:0000269|PubMed:15611160, CC ECO:0000269|PubMed:33164986}. CC -!- SUBUNIT: Interacts with the COPII coat components Sec23 (SEC23A and/or CC SEC23B) and Sec24 (SEC24A and/or SEC24B) (PubMed:11489904). Interacts CC with YIF1A (PubMed:15990086). May interact with RAB1A CC (PubMed:15611160). Interacts with YIPF3 and YIPF4 (PubMed:27999994). CC {ECO:0000269|PubMed:11489904, ECO:0000269|PubMed:15611160, CC ECO:0000269|PubMed:15990086, ECO:0000269|PubMed:27999994}. CC -!- INTERACTION: CC Q969M3; O75460: ERN1; NbExp=3; IntAct=EBI-2124787, EBI-371750; CC Q969M3; O95070: YIF1A; NbExp=8; IntAct=EBI-2124787, EBI-2799703; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9EQQ2}; Multi-pass membrane protein. Golgi CC apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:27999994}; CC Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle CC {ECO:0000250|UniProtKB:Q5XID0}. Note=Enriched at the endoplasmic CC reticulum exit sites (By similarity). Incorporated into COPII-coated CC vesicles (By similarity). {ECO:0000250|UniProtKB:Q5XID0, CC ECO:0000250|UniProtKB:Q9EQQ2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q969M3-1; Sequence=Displayed; CC Name=2; Synonyms=D; CC IsoId=Q969M3-2; Sequence=VSP_018253; CC Name=3; Synonyms=I; CC IsoId=Q969M3-3; Sequence=VSP_018254; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with abundant expression in CC pancreatic tissue, islets, beta cells, and brain. Highly expressed in CC coronary smooth muscles. {ECO:0000269|PubMed:15922870, CC ECO:0000269|PubMed:33164986}. CC -!- DEVELOPMENTAL STAGE: Expressed in developing cortex at all stages CC examined but most strikingly at 12 gestational weeks. Expression is CC found in both progenitor (ventricular zone) and neuronal (intermediate CC zone and cortical plate) compartments. Also selectively expressed CC within the choroid plexus within the cerebral ventricles. CC {ECO:0000269|PubMed:33164986}. CC -!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:15922870}. CC -!- DISEASE: Microcephaly, epilepsy, and diabetes syndrome 2 (MEDS2) CC [MIM:619278]: An autosomal recessive disorder characterized by neonatal CC or early-onset diabetes, severe microcephaly, and epilepsy. CC {ECO:0000269|PubMed:33164986}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF140225; AAG48521.1; -; mRNA. DR EMBL; AY640925; AAV51256.1; -; mRNA. DR EMBL; AY640926; AAV51257.1; -; mRNA. DR EMBL; AY640927; AAV51258.1; -; mRNA. DR EMBL; AY640928; AAV51259.1; -; mRNA. DR EMBL; AY640929; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AY640934; AAV51260.1; -; mRNA. DR EMBL; AY037152; AAK67644.1; -; mRNA. DR EMBL; AY358863; AAQ89222.1; -; mRNA. DR EMBL; AK054576; BAB70763.1; -; mRNA. DR EMBL; AF318329; AAL55836.1; -; mRNA. DR EMBL; AK223515; BAD97235.1; -; mRNA. DR EMBL; CR749463; CAH18295.1; -; mRNA. DR EMBL; CH471062; EAW61864.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61865.1; -; Genomic_DNA. DR EMBL; BC007829; AAH07829.1; -; mRNA. DR EMBL; BC014253; AAH14253.1; -; mRNA. DR EMBL; BC024737; AAH24737.1; -; mRNA. DR EMBL; AB014733; BAB20270.1; -; mRNA. DR CCDS; CCDS4279.1; -. [Q969M3-1] DR CCDS; CCDS64277.1; -. [Q969M3-2] DR RefSeq; NP_001020118.1; NM_001024947.3. [Q969M3-1] DR RefSeq; NP_001258661.1; NM_001271732.1. [Q969M3-2] DR RefSeq; NP_110426.4; NM_030799.8. [Q969M3-1] DR AlphaFoldDB; Q969M3; -. DR BioGRID; 123519; 157. DR IntAct; Q969M3; 64. DR MINT; Q969M3; -. DR STRING; 9606.ENSP00000274496; -. DR iPTMnet; Q969M3; -. DR PhosphoSitePlus; Q969M3; -. DR SwissPalm; Q969M3; -. DR BioMuta; YIPF5; -. DR DMDM; 74760683; -. DR EPD; Q969M3; -. DR jPOST; Q969M3; -. DR MassIVE; Q969M3; -. DR MaxQB; Q969M3; -. DR PaxDb; 9606-ENSP00000274496; -. DR PeptideAtlas; Q969M3; -. DR ProteomicsDB; 75792; -. [Q969M3-1] DR ProteomicsDB; 75793; -. [Q969M3-2] DR ProteomicsDB; 75794; -. [Q969M3-3] DR Pumba; Q969M3; -. DR Antibodypedia; 45624; 125 antibodies from 21 providers. DR DNASU; 81555; -. DR Ensembl; ENST00000274496.10; ENSP00000274496.5; ENSG00000145817.17. [Q969M3-1] DR Ensembl; ENST00000448443.6; ENSP00000397704.2; ENSG00000145817.17. [Q969M3-1] DR Ensembl; ENST00000513112.5; ENSP00000425422.1; ENSG00000145817.17. [Q969M3-2] DR GeneID; 81555; -. DR KEGG; hsa:81555; -. DR MANE-Select; ENST00000274496.10; ENSP00000274496.5; NM_030799.9; NP_110426.4. DR UCSC; uc003lnk.6; human. [Q969M3-1] DR AGR; HGNC:24877; -. DR CTD; 81555; -. DR DisGeNET; 81555; -. DR GeneCards; YIPF5; -. DR HGNC; HGNC:24877; YIPF5. DR HPA; ENSG00000145817; Low tissue specificity. DR MalaCards; YIPF5; -. DR MIM; 611483; gene. DR MIM; 619278; phenotype. DR neXtProt; NX_Q969M3; -. DR OpenTargets; ENSG00000145817; -. DR Orphanet; 306558; Primary microcephaly-epilepsy-permanent neonatal diabetes syndrome. DR PharmGKB; PA142670548; -. DR VEuPathDB; HostDB:ENSG00000145817; -. DR eggNOG; KOG3103; Eukaryota. DR GeneTree; ENSGT00940000153168; -. DR HOGENOM; CLU_074741_2_0_1; -. DR InParanoid; Q969M3; -. DR OMA; HIRAKSM; -. DR OrthoDB; 37764at2759; -. DR PhylomeDB; Q969M3; -. DR TreeFam; TF313100; -. DR PathwayCommons; Q969M3; -. DR SignaLink; Q969M3; -. DR BioGRID-ORCS; 81555; 95 hits in 1159 CRISPR screens. DR ChiTaRS; YIPF5; human. DR GeneWiki; YIPF5; -. DR GenomeRNAi; 81555; -. DR Pharos; Q969M3; Tbio. DR PRO; PR:Q969M3; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q969M3; Protein. DR Bgee; ENSG00000145817; Expressed in jejunal mucosa and 201 other cell types or tissues. DR ExpressionAtlas; Q969M3; baseline and differential. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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; IMP: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:UniProtKB. DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central. DR InterPro; IPR045231; Yip1/4-like. DR InterPro; IPR006977; Yip1_dom. DR PANTHER; PTHR21236; GOLGI MEMBRANE PROTEIN YIP1; 1. DR PANTHER; PTHR21236:SF6; PROTEIN YIPF5; 1. DR Pfam; PF04893; Yip1; 1. DR Genevisible; Q969M3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasmic vesicle; Diabetes mellitus; KW Disease variant; Endoplasmic reticulum; Epilepsy; 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_0000234328" FT TOPO_DOM 1..124 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:27999994" 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 VAR_SEQ 1..54 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15922870" FT /id="VSP_018253" FT VAR_SEQ 242..257 FT /note="YPCALLYGVFALISVF -> LQPNITYGSNYFLFCCLPYPQQHF (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:15922870" FT /id="VSP_018254" FT VARIANT 97 FT /note="G -> V (in MEDS2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33164986" FT /id="VAR_085533" FT VARIANT 98 FT /note="I -> S (in MEDS2; no effect on differentiation and FT function of pancreatic beta cells; increased endoplasmic FT reticulum stress-induced apoptosis; decreased in C-peptide FT levels associated with increased proinsulin accumulation)" FT /evidence="ECO:0000269|PubMed:33164986" FT /id="VAR_085534" FT VARIANT 106 FT /note="Missing (in MEDS2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33164986" FT /id="VAR_085535" FT VARIANT 181 FT /note="A -> V (in MEDS2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33164986" FT /id="VAR_085536" FT VARIANT 218 FT /note="W -> R (in MEDS2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33164986" FT /id="VAR_085537" FT CONFLICT 136..138 FT /note="AFG -> DLA (in Ref. 3; AAK67644)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="I -> S (in Ref. 1; AAG48521)" FT /evidence="ECO:0000305" FT CONFLICT 187 FT /note="C -> W (in Ref. 3; AAK67644)" FT /evidence="ECO:0000305" FT CONFLICT 192 FT /note="I -> Y (in Ref. 1; AAG48521)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="C -> R (in Ref. 7; BAD97235)" FT /evidence="ECO:0000305" SQ SEQUENCE 257 AA; 27989 MW; B30EACB0E514DC67 CRC64; MSGFENLNTD FYQTSYSIDD QSQQSYDYGG SGGPYSKQYA GYDYSQQGRF VPPDMMQPQQ PYTGQIYQPT QAYTPASPQP FYGNNFEDEP PLLEELGINF DHIWQKTLTV LHPLKVADGS IMNETDLAGP MVFCLAFGAT LLLAGKIQFG YVYGISAIGC LGMFCLLNLM SMTGVSFGCV ASVLGYCLLP MILLSSFAVI FSLQGMVGII LTAGIIGWCS FSASKIFISA LAMEGQQLLV AYPCALLYGV FALISVF //