ID   RIP_HUMAN      STANDARD;      PRT;   671 AA.
AC   Q13546; Q13180;
DT   01-NOV-1997 (Rel. 35, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   20-AUG-2001 (Rel. 40, Last annotation update)
DE   SERINE/THREONINE PROTEIN KINASE RIP (EC 2.7.1.-) (CELL DEATH PROTEIN
DE   RIP) (RECEPTOR INTERACTING PROTEIN).
GN   RIPK1 OR RIP.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Umbilical vein endothelial cells;
RX   MEDLINE=96200892; PubMed=8612133;
RA   Hsu H., Huang J., Shu H.-B., Baichwal V.R., Goeddel D.V.;
RT   "TNF-dependent recruitment of the protein kinase RIP to the TNF
RT   receptor-1 signaling complex.";
RL   Immunity 4:387-396(1996).
RN   [2]
RP   REVISION TO 120.
RA   Huang J., Hsu H., Baichwal V.R., Goeddel D.V.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE OF 300-671 FROM N.A.
RX   MEDLINE=95277838; PubMed=7538908;
RA   Stanger B.Z., Leder P., Lee T.-H., Kim E., Seed B.;
RT   "RIP: a novel protein containing a death domain that interacts with
RT   Fas/APO-1 (CD95) in yeast and causes cell death.";
RL   Cell 81:513-523(1995).
CC   -!- FUNCTION: INTERACTS WITH THE DEATH DOMAIN OF FAS AND TRADD AND
CC       INITIATES APOPTOSIS. IT IS RECRUITED BY TRADD TO TNFR1 IN A TNF-
CC       DEPENDENT PROCESS. REQUIRED FOR TNFR1 ACTIVATION OF NF-KAPPA B.
CC   -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES.
CC   -!- SIMILARITY: CONTAINS 1 DEATH DOMAIN.
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DR   EMBL; U50062; AAC32232.1; -.
DR   EMBL; U25994; AAC50137.1; -.
DR   HSSP; P11362; 1FGI.
DR   MIM; 603453; -.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR000719; Euk_pkinase.
DR   InterPro; IPR002290; Ser_thr_kin_actsite.
DR   InterPro; IPR001245; Tyr_kin.
DR   Pfam; PF00531; death; 1.
DR   Pfam; PF00069; pkinase; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00221; STYKc; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
KW   Transferase; Serine/threonine-protein kinase; ATP-binding;
KW   Apoptosis.
FT   DOMAIN       17    289       PROTEIN KINASE.
FT   NP_BIND      23     31       ATP (BY SIMILARITY).
FT   BINDING      49     49       ATP (BY SIMILARITY).
FT   ACT_SITE    138    138       BY SIMILARITY.
FT   DOMAIN      583    669       DEATH.
FT   DOMAIN      411    414       POLY-ARG.
FT   CONFLICT    514    514       T -> S (IN REF. 3).
SQ   SEQUENCE   671 AA;  75958 MW;  BADC4E7E70456ABE CRC64;
     MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG PNCIEHNEAL
     LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL MHVLKAEMST PLSVKGRIIL
     EIIEGMCYLH GKGVIHKDLK PENILVDNDF HIKIADLGLA SFKMWSKLNN EEHNELREVD
     GTAKKNGGTL YYMAPEHLND VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC
     IKSGNRPDVD DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED
     VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG MGPVEESWFA
     PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR QNVAYNREEE RRRRVSHDPF
     AQQRPYENFQ NTEGKGTVYS SAASHGNAVH QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD
     PGTAGPRVWY RPIPSHMPSL HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ
     IGAYNYMEIG GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN
     CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA QALHQCSRID
     LLSSLIYVSQ N
//