KRI1_BOVIN
ID KRI1_BOVIN Reviewed; 705 AA.
AC Q0V8M0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Protein KRI1 homolog;
GN Name=KRI1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- SIMILARITY: Belongs to the KRI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG67037.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BT026198; ABG67037.1; ALT_INIT; mRNA.
DR RefSeq; NP_001103542.1; NM_001110072.1.
DR AlphaFoldDB; Q0V8M0; -.
DR SMR; Q0V8M0; -.
DR STRING; 9913.ENSBTAP00000014206; -.
DR PaxDb; Q0V8M0; -.
DR PRIDE; Q0V8M0; -.
DR Ensembl; ENSBTAT00000014206; ENSBTAP00000014206; ENSBTAG00000010729.
DR GeneID; 511427; -.
DR KEGG; bta:511427; -.
DR CTD; 65095; -.
DR VEuPathDB; HostDB:ENSBTAG00000010729; -.
DR VGNC; VGNC:30713; KRI1.
DR eggNOG; KOG2409; Eukaryota.
DR GeneTree; ENSGT00390000005605; -.
DR HOGENOM; CLU_009647_0_1_1; -.
DR InParanoid; Q0V8M0; -.
DR OMA; QWRKETF; -.
DR OrthoDB; 572360at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000010729; Expressed in blood and 105 other tissues.
DR ExpressionAtlas; Q0V8M0; baseline and differential.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR InterPro; IPR018034; Kri1.
DR InterPro; IPR024626; Kri1-like_C.
DR PANTHER; PTHR14490; PTHR14490; 1.
DR Pfam; PF05178; Kri1; 1.
DR Pfam; PF12936; Kri1_C; 1.
PE 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..705
FT /note="Protein KRI1 homolog"
FT /id="PRO_0000298975"
FT REGION 31..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..705
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDQ9"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9T8"
SQ SEQUENCE 705 AA; 82540 MW; 20E09831FBD4C819 CRC64;
MPEPRGSSPL RVNAAFAARY GRYREREELQ RLKDRYGDRH SSSDSSSESD SSDEHVEFDP
QQERDFYRTL SLLKKKDPRI YQKDATFYQR TASSSDSEEE PAAEKRKKVQ PMYLKDYERK
VILEKGGKYV DEENSDGETS NQRLQQSSSK SYVEEQKQLK ESFRAFVEDS EDEDSAEEGG
SGLLQKRAKS KEEKAQEDAD YIEWLKGQKE IQNPDTLKEL THLREFWNNP ELDEGERFLR
DYILNKRYEE EGEEEDEEEE DEEEERVPGP PVQLAVDDSS DEGELFLKKQ EDFELKYNFR
FEEPDSASVK TYPRSIASSV RRKDERRKEK REETRERKKR EKARKQEELK QLKNLKRKEI
LAKLERLRQV TGNETLGFEE QDLEGDFDPA RHDQLMQKCF GDEYYGAMEE EKPQFEEEEG
LEDDWNWDTW AGPEQGGAWS QQEPHCEDPD FNMDADYDPS QPRKKQREAP SLGKKKRKSP
FATAVGQEKP VFDPGDKTFE EYLDEYYRLD YEDIIDDLPC RFKYRTVVPC DFGLSTEEIL
AADDKELNRW CSLKKTCMYR SEQEELQDKR VYSQKARNVW KKQQIFKSLC PEEAEMPTEA
TGKPQRDRAG SSGQLVAPDG ACGKRSQPES TPAEEEADPV TPTEKLAPQR RKRGKKARLL
GPTVTLGGRE FSRQRLQAFG LNPKRLHFRQ LGRQRRKQQG PKSSH
