ELAP1_MOUSE
ID ELAP1_MOUSE Reviewed; 1009 AA.
AC A2AFS3; A2AFS2; Q3UTM2; Q69ZL9; Q7TS96; Q8R215;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Endosome/lysosome-associated apoptosis and autophagy regulator 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=Elapor1 {ECO:0000312|MGI:MGI:1923930};
GN Synonyms=Kiaa1324 {ECO:0000312|EMBL:BAD32427.1};
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] (ISOFORM 3).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 438-1009.
RC STRAIN=FVB/N; TISSUE=Colon, and Eye;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, 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: May protect cells from cell death by inducing cytosolic
CC vacuolization and up-regulating the autophagy pathway. May play a role
CC in apoptosis and cell proliferation through its interaction with HSPA5.
CC {ECO:0000250|UniProtKB:Q6UXG2}.
CC -!- SUBUNIT: Interacts with HSPA5; may regulate the function of HSPA5 in
CC apoptosis and cell proliferation. {ECO:0000250|UniProtKB:Q6UXG2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6UXG2};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6UXG2}.
CC Late endosome membrane {ECO:0000250|UniProtKB:Q6UXG2}; Single-pass type
CC I membrane protein {ECO:0000250|UniProtKB:Q6UXG2}. Golgi apparatus,
CC trans-Golgi network membrane {ECO:0000250|UniProtKB:Q6UXG2}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q6UXG2}. Lysosome
CC membrane {ECO:0000250|UniProtKB:Q6UXG2}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6UXG2}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6UXG2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q6UXG2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AFS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AFS3-2; Sequence=VSP_025119, VSP_025120;
CC Name=3;
CC IsoId=A2AFS3-3; Sequence=VSP_025118, VSP_025120;
CC -!- SIMILARITY: Belongs to the ELAPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32427.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK173149; BAD32427.1; ALT_FRAME; mRNA.
DR EMBL; AK139330; BAE23958.1; -; mRNA.
DR EMBL; AL672200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL683823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022655; AAH22655.1; -; mRNA.
DR EMBL; BC051424; AAH51424.1; -; mRNA.
DR CCDS; CCDS17761.1; -. [A2AFS3-2]
DR RefSeq; NP_001028476.1; NM_001033304.1. [A2AFS3-2]
DR RefSeq; XP_006501477.1; XM_006501414.3. [A2AFS3-2]
DR RefSeq; XP_006501478.1; XM_006501415.3. [A2AFS3-2]
DR AlphaFoldDB; A2AFS3; -.
DR STRING; 10090.ENSMUSP00000102236; -.
DR GlyConnect; 2435; 1 N-Linked glycan (2 sites). [A2AFS3-2]
DR GlyGen; A2AFS3; 3 sites.
DR iPTMnet; A2AFS3; -.
DR PhosphoSitePlus; A2AFS3; -.
DR MaxQB; A2AFS3; -.
DR PaxDb; A2AFS3; -.
DR PeptideAtlas; A2AFS3; -.
DR PRIDE; A2AFS3; -.
DR Antibodypedia; 33748; 183 antibodies from 26 providers.
DR Ensembl; ENSMUST00000048012; ENSMUSP00000040128; ENSMUSG00000040412. [A2AFS3-2]
DR GeneID; 229722; -.
DR KEGG; mmu:229722; -.
DR UCSC; uc008qzd.1; mouse. [A2AFS3-2]
DR CTD; 57535; -.
DR MGI; MGI:1923930; Elapor1.
DR VEuPathDB; HostDB:ENSMUSG00000040412; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156861; -.
DR InParanoid; A2AFS3; -.
DR OMA; RYFHRFN; -.
DR PhylomeDB; A2AFS3; -.
DR TreeFam; TF315906; -.
DR BioGRID-ORCS; 229722; 0 hits in 60 CRISPR screens.
DR PRO; PR:A2AFS3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A2AFS3; protein.
DR Bgee; ENSMUSG00000040412; Expressed in prostate gland ventral lobe and 145 other tissues.
DR ExpressionAtlas; A2AFS3; baseline and differential.
DR Genevisible; A2AFS3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISO:MGI.
DR GO; GO:0044090; P:positive regulation of vacuole organization; ISO:MGI.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR039181; EIG121-like.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR PANTHER; PTHR22727; PTHR22727; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Lysosome;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1009
FT /note="Endosome/lysosome-associated apoptosis and autophagy
FT regulator 1"
FT /id="PRO_0000286601"
FT TOPO_DOM 36..906
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 907..927
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 928..1009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 652..854
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 988..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 274..291
FT /evidence="ECO:0000250"
FT DISULFID 304..326
FT /evidence="ECO:0000250"
FT DISULFID 307..338
FT /evidence="ECO:0000250"
FT DISULFID 654..700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 710..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 804..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 816..852
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VAR_SEQ 1..220
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_025118"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025119"
FT VAR_SEQ 228
FT /note="W -> WEFHS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025120"
FT CONFLICT 230
FT /note="E -> D (in Ref. 1; BAD32427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1009 AA; 110682 MW; 03BB5217A69FA85A CRC64;
MAEPGHNPHP SARDGGKTER RTPRLLWLLL WAGTTFQVTL GTGPELHACK ESEYHFEYTA
CDSTGSRWRV AVPHSPGLCT SLPDPVKGTE CSFSCNAGEF LDMKDQSCKP CAEGRYSLGT
GIRFDEWDEL PHGFASLSAN LEVDDSISES TENCTSSKWV PRGDYIASNT DECTATLMYA
VNLKQSGTVN FEYYYPDSSI IFEFFVQNDQ CQPSADDSRW MKTTEKGWVE LNRGNNVLYW
RTTAFSVWSK VSKPVLVRNI AITGVAYTSE CFPCKPGTYA AKQGSPFCKL CPANYYSNKG
ETSCHPCDAD KYSEKGSSTC KVRPACTDKD YFYTHTACDA QGETQLMYKW AIPKICGEDL
EGAVKLPASG VKTRCPPCNP GFFKTDNSTC EPCPYGSYSN GSDCTHCPAG TEPAVGFEYK
WWNTLPSNME TTVLSGINFE YKGLTGWEVA GDHIYTAVGA SDNDFMILTL VVPGFRPPQS
VVADTENKEV ARITFVFETI CSVNCELYFM VGMNSRTNTP VETWKGTKGK QSYTYTIEEN
ATVSFTWAFQ RTTLHETGRK YTNDVAKIYS INVTNVMGGV ASYCRPCALE ASDLGSSCTS
CPAGHYINRD SGTCHLCPSN TILKAHQPYG AQACVPCGPG TKNNKIHSLC YNDCTFSRNT
PSRIFNYNFS ALAGTVSLAG VPSFTSKGLK YFHHFTLSLC GNQGKKMAVC TDNVTDLRIP
DGEAGFSKSV TAYVCQVVII PSEVMGYKAG VSSQPVSLAD RLVGVSTDMT LEGIVSPVEL
FHPETSGIPD IVFFFRSNDV TQSCSSGRST TIRLRCNPMK AAPGTLRLPS MCSDGTCDGC
NFHFLWESVA ACPLCSASDY HTFVSSCVAG IQKTTYMWRE PKLCSGGISL PEQRVTICKT
IDFWLKVGIS AGTCTAILLT VLTCYFWKKN QKLEYKYSKL VMNATLKDCD LPAADSCAIM
EGEDVEDDFI FTSKKSLFGK IKSFTSKRTP DGFDSVPLKT SSGGPDMDM
