GP42_RAT
ID GP42_RAT Reviewed; 233 AA.
AC P23505;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Cell surface glycoprotein gp42;
DE Flags: Precursor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1845873; DOI=10.1084/jem.173.1.251;
RA Seaman W.E., Niemi E.C., Stark M.R., Goldfien R.D., Pollock A.S.,
RA Imboden J.B.;
RT "Molecular cloning of gp42, a cell-surface molecule that is selectively
RT induced on rat natural killer cells by interleukin 2: glycolipid membrane
RT anchoring and capacity for transmembrane signaling.";
RL J. Exp. Med. 173:251-260(1991).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: NK cells.
CC -!- INDUCTION: By interleukin-2.
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DR EMBL; X56448; CAA39831.1; -; mRNA.
DR PIR; JH0372; JH0372.
DR AlphaFoldDB; P23505; -.
DR SMR; P23505; -.
DR STRING; 10116.ENSRNOP00000000059; -.
DR GlyGen; P23505; 3 sites.
DR PaxDb; P23505; -.
DR UCSC; RGD:1563939; rat.
DR RGD; 1563939; LOC305103.
DR eggNOG; ENOG502RU0I; Eukaryota.
DR InParanoid; P23505; -.
DR PhylomeDB; P23505; -.
DR PRO; PR:P23505; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042289; F:MHC class II protein binding; ISO:RGD.
DR GO; GO:0019902; F:phosphatase binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13895; Ig_2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..16
FT CHAIN 17..206
FT /note="Cell surface glycoprotein gp42"
FT /id="PRO_0000014768"
FT PROPEP 207..233
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014769"
FT DOMAIN 23..98
FT /note="Ig-like 1"
FT DOMAIN 115..195
FT /note="Ig-like 2"
FT LIPID 206
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 136..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 215
FT /note="V -> M (in clone 2)"
SQ SEQUENCE 233 AA; 26025 MW; E6A03816FE151C59 CRC64;
MLLWMVLLLC VSMTEAQELF QDPVLSRLNS SETSDLLLKC TTKVDPNKPA SELFYSFYKD
NHIIQNRSHN PLFFISEANE ENSGLYQCVV DAKDGTIQKK SDYLDIDLCT SVSQPVLTLQ
HEATNLAEGD KVKFLCETQL GSLPILYSFY MDGEILGEPL APSGRAASLL ISVKAEWSGK
NYSCQAENKV SRDISEPKKF PLVVSGTASM KSTTVVIWLP VSCLVGWPWL LRF
