ID   INSR$HUMAN     STANDARD;      PRT;  1382 AA.
AC   P06213;
DT   01-JAN-1988  (REL. 06, CREATED)
DT   01-JAN-1988  (REL. 06, LAST SEQUENCE UPDATE)
DT   01-MAR-1989  (REL. 10, LAST ANNOTATION UPDATE)
DE   INSULIN RECEPTOR PRECURSOR (EC 2.7.1.112).
OS   HUMAN (HOMO SAPIENS).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1] (SEQUENCE FROM N.A.)
RA   EBINA Y., ELLIS L., JARNAGIN K., EDERY M., GRAF L., CLAUSER E.,
RA   OU J.-H., MASIARZ F., KAN Y.W., GOLDFINE I.D., ROTH R.A., RUTTER W.J.;
RL   CELL 40:747-758(1985).
RN   [2] (SEQUENCE FROM N.A.)
RA   ULLRICH A., BELL J.R., CHEN E.Y., HERRERA R., PETRUZZELLI L.M.,
RA   DULL T.J., GRAY A., COUSSENS L., LIAO Y.-C., TSUBOKAWA M.,
RA   MASON A., SEEBURG P.H., GRUNFELD C., ROSEN O.M., RAMACHANDRAN J.;
RL   NATURE 313:756-761(1985).
RN   [3] (REVISION TO 899-900)
RA   CHEN E.Y.;
RL   SUBMITTED (JUL-1985) TO EMBL/GENBANK DATA BANKS.
RN   [4] (SEQUENCE OF TRYPTIC PEPTIDES)
RA   FUJITA-YAMAGUCHI Y., HAWKE D., SHIVELY J.E., CHOI S.;
RL   PROTEIN SEQ. DATA ANAL. 1:3-6(1987).
RN   [5] (MUTATION OF 999)
RA   WHITE M.F., LIVINGSTON J.N., BACKER J.M., LAURIS V., DULL T.J.,
RA   ULLRICH A., KAHN C.R.;
RL   CELL 54:641-649(1988).
RN   [6] (MUTATION OF 1057)
RA   EBINA Y., ARAKI E., TAIRA M., SHIMADA F., MORI M., CRAIK C.S.,
RA   SIDDLE K., PIERCE S.B., ROTH R.A., RUTTER W.J.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 84:704-708(1987).
CC   -!- FUNCTION: THIS RECEPTOR BINDS INSULIN AND HAS A TYROSINE-PROTEIN
CC       KINASE ACTIVITY.
CC   -!- AFTER BEING TRANSPORTED FROM THE ENDOPLASMIC RETICULUM TO THE
CC       GOLGI APPARATUS, THE SINGLE GLYCOSYLATED PRECURSOR IS FURTHER
CC       GLYCOSYLATED AND THEN CLEAVED, FOLLOWED BY ITS TRANSPORT TO
CC       THE PLASMA MEMBRANE.
CC   -!- SUBUNIT: TETRAMER OF 2 ALPHA AND 2 BETA CHAINS LINKED BY DISULFIDE
CC       BONDS. THE ALPHA CHAINS CONTRIBUTE TO THE FORMATION OF THE LIGAND-
CC       BINDING DOMAIN, WHILE THE BETA CHAIN CARRY THE KINASE DOMAIN.
CC   -!- AUTOPHOSPHORYLATION ACTIVATES THE KINASE ACTIVITY.
CC   -!- SIMILARITY: BELONGS TO THE INSULIN RECEPTOR FAMILY OF TYROSINE-
CC       PROTEIN KINASES.
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DR   EMBL; M10051; HSINSR.
DR   EMBL; X02160; HSIRPR.
KW   TRANSFERASE; TYROSINE-PROTEIN KINASE; RECEPTOR; TRANSMEMBRANE;
KW   GLYCOPROTEIN; ATP-BINDING; PHOSPHORYLATION; SIGNAL.
FT   SIGNAL        1     27
FT   CHAIN        28    762       ALPHA-SUBUNIT.
FT   CHAIN       763   1382       BETA-SUBUNIT.
FT   DOMAIN      763    956       EXTRACELLULAR (PUTATIVE).
FT   TRANSMEM    957    979       PUTATIVE.
FT   DOMAIN      980   1382       CYTOPLASMIC (CATALYTIC).
FT   NP_BIND    1030   1035       ATP (BY SIMILARITY).
FT   BINDING    1057   1057       ATP.
FT   MUTAGEN    1057   1057       K->A,M,R: ABOLISH THE KINASE ACTIVITY.
FT   MOD_RES    1189   1189       PHOSPHORYLATION (AUTO-).
FT   ACT_SITE    999    999       IMPORTANT FOR BIOLOGICAL ACTIVITY.
FT   MUTAGEN     999    999       Y->F: HAS NO EFFECT ON INSULIN-STIMULATED
FT                                AUTOPHOSPHORYLATION, BUT INHIBITS THE
FT                                BIOLOGICAL ACTIVITY OF THE RECEPTOR.
FT   CARBOHYD     43     43       POTENTIAL.
FT   CARBOHYD     52     52       POTENTIAL.
FT   CARBOHYD    105    105       POTENTIAL.
FT   CARBOHYD    138    138       POTENTIAL.
FT   CARBOHYD    242    242       POTENTIAL.
FT   CARBOHYD    282    282       POTENTIAL.
FT   CARBOHYD    322    322       POTENTIAL.
FT   CARBOHYD    364    364       POTENTIAL.
FT   CARBOHYD    424    424       POTENTIAL.
FT   CARBOHYD    445    445       POTENTIAL.
FT   CARBOHYD    541    541       POTENTIAL.
FT   CARBOHYD    633    633       POTENTIAL.
FT   CARBOHYD    651    651       POTENTIAL.
FT   CARBOHYD    698    698       POTENTIAL.
FT   CARBOHYD    769    769       POTENTIAL.
FT   CARBOHYD    782    782       POTENTIAL.
FT   CARBOHYD    920    920       POTENTIAL.
FT   CARBOHYD    933    933       POTENTIAL.
FT   CONFLICT    171    171       H -> Y (IN REF. 2).
FT   CONFLICT    448    448       T -> I (IN REF. 2).
FT   CONFLICT    492    492       K -> Q (IN REF. 2).
FT   CONFLICT    601    601       D -> N (IN REF. 4).
FT   CONFLICT    745    756       MISSING (IN REF. 2).
FT   CONFLICT    830    830       P -> E (IN REF. 4).
FT   CONFLICT   1278   1278       K -> N (IN REF. 2).
SQ   SEQUENCE   1382 AA;  156279 MW;  1.00628E+07 CN;
     MGTGGRRGAA AAPLLVAVAA LLLGAAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL
     QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL
     VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN HIVLNKDDNE
     ECGDICPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHSECL
     GNCSQPDDPT KCVACRNFYL DGRCVETCPP PYYHFQDWRC VNFSFCQDLH HKCKNSRRQG
     CHQYVIHNNK CIPECPSGYT MNSSNLLCTP CLGPCPKVCH LLEGEKTIDS VTSAQELRGC
     TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGYLKIRRS YALVSLSFFR KLRLIRGETL
     EIGNYSFYAL DNQNLRQLWD WSKHNLTTTQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE
     RNDIALKTNG DKASCENELL KFSYIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ
     NVTEFDGQDA CGSNSWTVVD IDPPLRSNDP KSQNHPGWLM RGLKPWTQYA IFVKTLVTFS
     DERRTYGAKS DIIYVQTDAT NPSVPLDPIS VSNSSSQIIL KWKPPSDPNG NITHYLVFWE
     RQAEDSELFE LDYCLKGLKL PSRTWSPPFE SEDSQKHNQS EYEDSAGECC SCPKTDSQIL
     KELEESSFRK TFEDYLHNVV FVPRKTSSGT GAEDPRPSRK RRSLGDVGNV TVAVPTVAAF
     PNTSSTSVPT SPEEHRPFEK VVNKESLVIS GLRHFTGYRI ELQACNQDTP EERCSVAAYV
     SARTMPEAKA DDIVGPVTHE IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV
     SRKHFALERG CRLRGLSPGN YSVRIRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG
     PLIFVFLFSV VIGSIYLFLR KRQPDGPLGP LYASSNPEYL SASDVFPCSV YVPDEWEVSR
     EKITLLRELG QGSFGMVYEG NARDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG
     FTCHHVVRLL GVVSKGQPTL VVMELMAHGD LKSYLRSLRP EAENNPGRPP PTLQEMIQMA
     AEIADGMAYL NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV
     RWMAPESLKD GVFTTSSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDQPDN
     CPERVTDLMR MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFHSEENK APESEELEME
     FEDMENVPLD RSSHCQREEA GGRDGGSSLG FKRSYEEHIP YTHMNGGKKN GRILTLPRSN
     PS
//