MIPR_LYMST
ID MIPR_LYMST Reviewed; 1607 AA.
AC Q25410;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative molluscan insulin-related peptide(s) receptor;
DE EC=2.7.10.1;
DE Contains:
DE RecName: Full=Putative molluscan insulin-related peptide(s) receptor alpha chain;
DE Contains:
DE RecName: Full=Putative molluscan insulin-related peptide(s) receptor beta chain;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=CNS;
RX PubMed=7557427; DOI=10.1016/0378-1119(95)00323-x;
RA Roovers E., Vincent M., van Kesteren E., Geraerts W.P.M., Planta R.J.,
RA Vreugdenhil E., van Heerikhuizen H.;
RT "Characterization of a putative molluscan insulin-related peptide
RT receptor.";
RL Gene 162:181-188(1995).
CC -!- FUNCTION: This receptor probably binds to the four different molluscan
CC insulin-related peptides and has a tyrosine-protein kinase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Probable tetramer of 2 alpha and 2 beta chains linked by
CC disulfide bonds. The alpha chains contribute to the formation of the
CC ligand-binding domain, while the beta chains carry the kinase domain
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X84994; CAA59353.1; -; mRNA.
DR PIR; T43212; T43212.
DR AlphaFoldDB; Q25410; -.
DR SMR; Q25410; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.80.20.20; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Kinase; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..694
FT /note="Putative molluscan insulin-related peptide(s)
FT receptor alpha chain"
FT /id="PRO_0000016708"
FT CHAIN 698..1607
FT /note="Putative molluscan insulin-related peptide(s)
FT receptor beta chain"
FT /id="PRO_0000016710"
FT TOPO_DOM 698..975
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 997..1607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 517..632
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 636..726
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 756..861
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 870..967
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1037..1308
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1328..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1043..1051
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1072
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1199
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1607 AA; 181821 MW; F9CD1AEB25D2EBD6 CRC64;
MHPGSISFNM IINKCIPICL FILFIMMMEF TVSKADSKND IVSESHPSLQ KLGCGGSQSP
TNGVCGSVDI RSSMDNFKLL ENCTVIEGSL RISLFELKAL DFRHLSFPDL REITDYLLMY
RVYGLETLSK LFPNLAIIRG RELFNSYAIV MYEMRDLQDL GLVNLRTISR GGVRLTKNFK
LCYIETINWT QIGVSDPEAR RFINNKEQCP NSCKDECQSK RCWTYSDCQK GLNCQCKENT
YCMENGSCCH DYCLGGCKVP MNPDECFSCK EVQFNNTCRP QCPPGTYKFL NRRCLTDKEC
LALTNDPDGN TPKLLDGEKG EPSLCLYTCP QNYSVGDSKD NKNLSQCVKC RQLCPKECHG
LEINNIQDAH KLKECSKISG PLKIQIMSGS NVAQELEKSL GNIREVTETI HIKRSYALVT
LHFFKNLQII GSKVPSSETQ EGQSFSLFLM DNTNLQELFP EEQMKKMKIL NGGIYVHDNG
QLCPHTIKEF LSHLNLSEAQ SSISSISNGH QRPCEKHDLN VTVEKIAHNA AILAWNKYKA
DERQLLTYIL NYKEIKDESN DINIFQGRDL CSHDLWMTRE YAPKEGPEAD QIGMLYDLKP
FTTYAVYIQA YTVSTATHAA MTNILTFTTY PFHPSEPTDL VAISEDPHEL RVSWKPPKYP
NGNITHYKIV YHKLELNEKS YEQRNYCRDP LVHQKKKEKV KIEEEGKKIN NSANSNCCKC
PKSKEEMDTE SRKREIEMYF EDYLHKHIYC KRYDKLPDEV DLNFDGMNLP QLVEMNYNSS
ETSDRIEVFP NYVIENTSDL ANLTEIVKEV VVYGTTEVTL PNLEHFSEYS IEVLACQDYN
EKVLSKLCSI RAITFERTKD SYAADMINET TVDTEIETNF TGNVFIKWES PTSPNGLILK
YLLWYKKANQ ENLVPQTICI TRQEYLKNLG YKLTRLEPGN WTFKISAISL AENSSFTLER
FFIVPRPPDP ESSNTLLIVA IVLAFFGVLT VSLIVACVYY KQKIRSDDMT VISRNMNYVP
SEILYISDEW EVDRDKIKLI KELGQGSFGM VYEGVAKGIR DDPNEEIPVA VKTVNDRASF
SDRREFLKEA TTMKEFHCHH VVKLLGVVST GQPALVIMEL MALGDLKNYL RGHRPDEDHP
GVMPPHLLDI LQMAGEIADG MAYLADKKFV HRDLAARNCM VSEERTVKIG DFGMTRDIYE
TDYYRKGGKG MLPVRWMAPE SLKDGVFTSL SDVWSYGVVM WEMVTLAAQP YQGLSNEEVV
KFISDGYIME LPENCPNEMA YLMQHCWAKK PNQRPTFKAI IEYLLPKLKP SFEKVSYFFT
SGGGHTDGAG EGTLAEPEGS DDSSSINSLS CEGAAAPRQS LTPCGGGQFK SSTHFNGGSH
TLYDEGVDRE TILNGVDDGD EDEAAGRYSL SEFGEDLDDS SRPFMSDDFI PPVMTRQPLL
SHQSNGNDSN VRNSGLIELK PLINKDKRPG LSSPRLNARS NPFSSEYIGH YPPTLTTELE
TLNGNQSSHN NNSFELMTPD PLKSGPASES SNGVSSSSWR PKPILKLPTL NQARVGDSVG
CLCLTLGTRI NIVKPIETVR PETNTIRYLK PPHPMLIWST LKMVLVL
