YIPF5_HUMAN
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 03-AUG-2022, entry version 151.
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}.
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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; 108.
DR IntAct; Q969M3; 62.
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; Q969M3; -.
DR PeptideAtlas; Q969M3; -.
DR PRIDE; Q969M3; -.
DR ProteomicsDB; 75792; -. [Q969M3-1]
DR ProteomicsDB; 75793; -. [Q969M3-2]
DR ProteomicsDB; 75794; -. [Q969M3-3]
DR Antibodypedia; 45624; 121 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 CTD; 81555; -.
DR DisGeNET; 81555; -.
DR GeneCards; YIPF5; -.
DR HGNC; HGNC:24877; YIPF5.
DR HPA; ENSG00000145817; Low tissue specificity.
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; IGINFDH; -.
DR OrthoDB; 1457080at2759; -.
DR PhylomeDB; Q969M3; -.
DR TreeFam; TF313100; -.
DR PathwayCommons; Q969M3; -.
DR SignaLink; Q969M3; -.
DR BioGRID-ORCS; 81555; 93 hits in 1081 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 199 other tissues.
DR ExpressionAtlas; Q969M3; baseline and differential.
DR Genevisible; Q969M3; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR21236; PTHR21236; 1.
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; unknown pathological
FT 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33164986"
FT /id="VAR_085535"
FT VARIANT 181
FT /note="A -> V (in MEDS2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33164986"
FT /id="VAR_085536"
FT VARIANT 218
FT /note="W -> R (in MEDS2; unknown pathological
FT 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
