GPA33_MOUSE
ID GPA33_MOUSE Reviewed; 319 AA.
AC Q9JKA5; Q922D5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Cell surface A33 antigen;
DE AltName: Full=Glycoprotein A33;
DE Short=mA33;
DE Flags: Precursor;
GN Name=Gpa33;
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].
RC TISSUE=Colon epithelium, and Small intestine mucosa;
RX PubMed=10960348; DOI=10.1152/ajpgi.2000.279.3.g500;
RA Johnstone C.N., Tebbutt N.C., Abud H.E., White S.J., Stenvers K.L.,
RA Hall N.E., Cody S.H., Whitehead R.H., Catimel B., Nice E.C., Burgess A.W.,
RA Heath J.K.;
RT "Characterization of mouse A33 antigen; a definitive marker for basolateral
RT surfaces of intestinal epithelial cells.";
RL Am. J. Physiol. 279:G500-G510(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: May play a role in cell-cell recognition and signaling.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
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; AF247659; AAF65818.1; -; mRNA.
DR EMBL; BC008528; AAH08528.1; -; mRNA.
DR CCDS; CCDS15447.1; -.
DR RefSeq; NP_067623.1; NM_021610.1.
DR AlphaFoldDB; Q9JKA5; -.
DR SMR; Q9JKA5; -.
DR STRING; 10090.ENSMUSP00000060147; -.
DR GlyGen; Q9JKA5; 4 sites.
DR PhosphoSitePlus; Q9JKA5; -.
DR MaxQB; Q9JKA5; -.
DR PaxDb; Q9JKA5; -.
DR PeptideAtlas; Q9JKA5; -.
DR PRIDE; Q9JKA5; -.
DR ProteomicsDB; 267754; -.
DR ABCD; Q9JKA5; 33 sequenced antibodies.
DR GeneID; 59290; -.
DR KEGG; mmu:59290; -.
DR UCSC; uc007dkj.1; mouse.
DR CTD; 10223; -.
DR MGI; MGI:1891703; Gpa33.
DR eggNOG; ENOG502QR0Y; Eukaryota.
DR InParanoid; Q9JKA5; -.
DR OrthoDB; 841952at2759; -.
DR PhylomeDB; Q9JKA5; -.
DR TreeFam; TF330875; -.
DR BioGRID-ORCS; 59290; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9JKA5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JKA5; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042474; A33.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR44969; PTHR44969; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..319
FT /note="Cell surface A33 antigen"
FT /id="PRO_0000014771"
FT TOPO_DOM 22..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..134
FT /note="Ig-like V-type"
FT DOMAIN 140..227
FT /note="Ig-like C2-type"
FT REGION 267..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 12
FT /note="L -> F (in Ref. 1; AAF65818)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="G -> S (in Ref. 1; AAF65818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35692 MW; A37C8DB4BF685C3A CRC64;
MLGKAGSVVW MLCAIWVAAD ALTVETTQDI LRAARGRSVT LPCTYNTYVS DREGFIQWDK
LLRSQTERVV TWNFVTKKYI YGNRYENRVR VSNDAELSNA SITIDQLTMD DNGTYECSVS
LMSDQDVNAK SRVRLLVLVP PSKPDCSIQG EMVIGNNIQL TCHSAEGSPS PQYSWKSYNA
QNQQRPLTQP VSGEPLLLKN ISTETAGYYI CTSSNDVGIE SCNITVAPRP PSMNIALYAG
IAGGVFVALI IIGVIVYCCC CREKDDKDQD REDARPNRAA YQVPKKEQKE ISRGREDEDD
HRHEDRWSSG RSTPDQPFQ
