ICA69_MOUSE
ID ICA69_MOUSE Reviewed; 478 AA.
AC P97411; E9QLS3; P97362; P97954; Q99M40; Q9R2C4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Islet cell autoantigen 1;
DE AltName: Full=69 kDa islet cell autoantigen;
DE Short=ICA69;
DE AltName: Full=Islet cell autoantigen p69;
DE Short=ICAp69;
DE Short=p69;
GN Name=Ica1 {ECO:0000312|MGI:MGI:96391}; Synonyms=Icap69;
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] (ISOFORMS 1 AND 2).
RC STRAIN=NOD; TISSUE=Brain;
RX PubMed=8975715; DOI=10.1006/geno.1996.0641;
RA Gaedigk R., Karges W., Hui M.F., Scherer S.W., Dosch H.-M.;
RT "Genomic organization and transcript analysis of ICAp69, a target antigen
RT in diabetic autoimmunity.";
RL Genomics 38:382-391(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Brain;
RX PubMed=9128175; DOI=10.1016/s0925-4439(97)00002-1;
RA Karges W.J.P., Gaedigk R., Hui M.F., Cheung R.K., Dosch H.-M.;
RT "Molecular cloning of murine ICA69: diabetes-prone mice recognize the human
RT autoimmune-epitope, Tep69, conserved in splice variants from both
RT species.";
RL Biochim. Biophys. Acta 1360:97-101(1997).
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] {ECO:0000305, ECO:0000312|EMBL:AAH02030.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH02030.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC99989.1}
RP NUCLEOTIDE SEQUENCE OF 6-478 (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAC99989.1};
RA Karges W.J.P., Gaedigk R., Hui M.F., Cheung R.K., Dosch H.-M.;
RT "Islet cell antigen p69 in non-obese diabetic mice: cloning, alternative
RT splicing, and demonstration of T cell cross-reactivity to bovine serum
RT albumin.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11029035; DOI=10.1091/mbc.11.10.3277;
RA Pilon M., Peng X.-R., Spence A.M., Plasterk R.H.A., Dosch H.-M.;
RT "The diabetes autoantigen ICA69 and its Caenorhabditis elegans homologue,
RT ric-19, are conserved regulators of neuroendocrine secretion.";
RL Mol. Biol. Cell 11:3277-3288(2000).
RN [7] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=11751995; DOI=10.4049/jimmunol.168.1.475;
RA Winer S., Astsaturov I., Gaedigk R., Hammond-McKibben D., Pilon M.,
RA Song A., Kubiak V., Karges W., Arpaia E., McKerlie C., Zucker P., Singh B.,
RA Dosch H.-M.;
RT "ICA69(null) nonobese diabetic mice develop diabetes, but resist disease
RT acceleration by cyclophosphamide.";
RL J. Immunol. 168:475-482(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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: May play a role in neurotransmitter secretion.
CC {ECO:0000303|PubMed:11029035}.
CC -!- INTERACTION:
CC P97411; Q62083: Pick1; NbExp=2; IntAct=EBI-16056188, EBI-77550;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11029035}.
CC Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Predominantly
CC cytosolic. Also exists as a membrane-bound form which has been found
CC associated with synaptic vesicles and also with the Golgi complex and
CC immature secretory granules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1 {ECO:0000269|PubMed:8975715}; Synonyms=Alpha
CC {ECO:0000303|PubMed:8975715};
CC IsoId=P97411-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8975715}; Synonyms=Beta
CC {ECO:0000303|PubMed:8975715};
CC IsoId=P97411-2; Sequence=VSP_050425, VSP_050426;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain, pancreas and
CC stomach mucosa. High expression also found in stomach muscle and
CC testis. {ECO:0000269|PubMed:11029035}.
CC -!- DISRUPTION PHENOTYPE: 129/SvJ mice lacking Ica1 do not display an
CC obvious phenotype and age normally, while NOD mice without Ica1 develop
CC diabetes and display sudden mid-life lethality but are resistant to
CC cyclophosphamide-induced disease acceleration.
CC {ECO:0000269|PubMed:11751995}.
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DR EMBL; U26459; AAC52992.1; -; mRNA.
DR EMBL; U26460; AAB40939.1; -; mRNA.
DR EMBL; U26461; AAC52993.1; -; mRNA.
DR EMBL; U37186; AAB19182.1; -; Genomic_DNA.
DR EMBL; U37013; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37014; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37015; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37082; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37083; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37084; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37085; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37086; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37184; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; U37185; AAB19182.1; JOINED; Genomic_DNA.
DR EMBL; AC158670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002030; AAH02030.1; -; mRNA.
DR EMBL; U34595; AAC99989.1; -; mRNA.
DR CCDS; CCDS19911.1; -. [P97411-1]
DR RefSeq; NP_001239195.1; NM_001252266.1. [P97411-2]
DR RefSeq; NP_034622.3; NM_010492.3. [P97411-1]
DR RefSeq; XP_006505056.1; XM_006504993.3. [P97411-1]
DR RefSeq; XP_006505057.1; XM_006504994.3. [P97411-1]
DR RefSeq; XP_006505058.1; XM_006504995.3. [P97411-2]
DR AlphaFoldDB; P97411; -.
DR BioGRID; 200500; 1.
DR DIP; DIP-60170N; -.
DR IntAct; P97411; 1.
DR STRING; 10090.ENSMUSP00000040062; -.
DR iPTMnet; P97411; -.
DR PhosphoSitePlus; P97411; -.
DR MaxQB; P97411; -.
DR PaxDb; P97411; -.
DR PRIDE; P97411; -.
DR ProteomicsDB; 269520; -. [P97411-1]
DR ProteomicsDB; 269521; -. [P97411-2]
DR Antibodypedia; 1895; 258 antibodies from 27 providers.
DR DNASU; 15893; -.
DR Ensembl; ENSMUST00000038403; ENSMUSP00000040062; ENSMUSG00000062995. [P97411-1]
DR Ensembl; ENSMUST00000115520; ENSMUSP00000111182; ENSMUSG00000062995. [P97411-1]
DR GeneID; 15893; -.
DR KEGG; mmu:15893; -.
DR UCSC; uc009axx.1; mouse. [P97411-2]
DR UCSC; uc009axy.1; mouse. [P97411-1]
DR CTD; 3382; -.
DR MGI; MGI:96391; Ica1.
DR VEuPathDB; HostDB:ENSMUSG00000062995; -.
DR eggNOG; KOG3891; Eukaryota.
DR GeneTree; ENSGT00390000005530; -.
DR InParanoid; P97411; -.
DR OMA; THNACSE; -.
DR OrthoDB; 766523at2759; -.
DR PhylomeDB; P97411; -.
DR TreeFam; TF317186; -.
DR BioGRID-ORCS; 15893; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ica1; mouse.
DR PRO; PR:P97411; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P97411; protein.
DR Bgee; ENSMUSG00000062995; Expressed in spermatid and 233 other tissues.
DR ExpressionAtlas; P97411; baseline and differential.
DR Genevisible; P97411; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0140090; F:membrane curvature sensor activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:InterPro.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; NAS:UniProtKB.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0051049; P:regulation of transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR010504; AH_dom.
DR InterPro; IPR030796; ICA1.
DR InterPro; IPR024114; Islet_autoAg_Ica1/Ica1-like.
DR InterPro; IPR006723; Islet_autoAg_Ica1_C.
DR PANTHER; PTHR10164; PTHR10164; 1.
DR PANTHER; PTHR10164:SF3; PTHR10164:SF3; 1.
DR Pfam; PF06456; Arfaptin; 1.
DR Pfam; PF04629; ICA69; 2.
DR SMART; SM01015; Arfaptin; 1.
DR SMART; SM01237; ICA69; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS50870; AH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW Membrane; Neurotransmitter transport; Reference proteome; Synapse;
KW Transport.
FT CHAIN 1..478
FT /note="Islet cell autoantigen 1"
FT /id="PRO_0000084131"
FT DOMAIN 50..253
FT /note="AH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT REGION 306..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 315
FT /note="T -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8975715"
FT /id="VSP_050425"
FT VAR_SEQ 316..336
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8975715"
FT /id="VSP_050426"
FT CONFLICT 170
FT /note="L -> F (in Ref. 1; AAB19182)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> T (in Ref. 1; AAB19182/AAC52992/AAC52993/
FT AAB40939, 4; AAH02030 and 5; AAC99989)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="Q -> R (in Ref. 1; AAB19182/AAC52992/AAC52993/
FT AAB40939, 4; AAH02030 and 5; AAC99989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54324 MW; B7B1EE18AC39E2F9 CRC64;
MSGHKCYSWE LQDRFAQDKS VVNKMQQKYW ETKQAFIKAT GKKEDEHVVA SDADLDAKLE
LFHSIQRTCL DLSKAIVLYQ KRICFLSQEE NELGKFLRSQ GFQDKTRAGK MMQATGKALC
FSSQQRLALR NPLCRFHQEV ETFRHRAISD TWLTVNRMEQ YRTEYRGALL WMKDVSQELD
PDLYKQMEKF RKVQTQVRLA KKNFDKLKMD VCQKVDLLGA SRCNLLSHML ATYQTTLLHF
WEKTSHTMAA IHESFKGYQP YEFTTLKSLQ DPMKKLVEKE GKKTSWRENR EAVAPEPRQL
ISLEDEHKDS SAYKTEEGTS VLSSVDKGSV HDTCSGPIDE LLDGKPEEAC LGPTAGTPEP
ESGDKDDLLL LNEIFSTSCL DEGEFSREWA AVFGDDQLKE PAPMGAQGEP DPKPQIGSGF
LPSQLLDQNM KDLQASLQEP AKAASDLTAW FSLFADLDPL SNPDAVGKTD KEHELLNA
