RRBP1_CANLF
ID RRBP1_CANLF Reviewed; 1534 AA.
AC Q28298;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Ribosome-binding protein 1;
DE AltName: Full=180 kDa ribosome receptor;
DE Short=RRp;
GN Name=RRBP1; Synonyms=P180;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=7790375; DOI=10.1083/jcb.130.1.29;
RA Wanker E.E., Sun Y., Savitz A.J., Meyer D.I.;
RT "Functional characterization of the 180 kDa ribosome receptor in vivo.";
RL J. Cell Biol. 130:29-39(1995).
CC -!- FUNCTION: Acts as a ribosome receptor and mediates interaction between
CC the ribosome and the endoplasmic reticulum membrane.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:7790375}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:7790375}.
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DR EMBL; X87224; CAA60676.1; -; mRNA.
DR PIR; A56734; A56734.
DR RefSeq; NP_001003179.1; NM_001003179.1.
DR AlphaFoldDB; Q28298; -.
DR SMR; Q28298; -.
DR BioGRID; 139730; 1.
DR STRING; 9612.ENSCAFP00000034278; -.
DR PRIDE; Q28298; -.
DR GeneID; 403809; -.
DR CTD; 6238; -.
DR eggNOG; KOG1999; Eukaryota.
DR InParanoid; Q28298; -.
DR OrthoDB; 327650at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR InterPro; IPR007794; Rib_rcpt_KP.
DR InterPro; IPR040248; RRBP1.
DR PANTHER; PTHR18939; PTHR18939; 2.
DR Pfam; PF05104; Rib_recp_KP_reg; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Isopeptide bond; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1534
FT /note="Ribosome-binding protein 1"
FT /id="PRO_0000097440"
FT TOPO_DOM 1..7
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..1534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 197..206
FT /note="1"
FT REPEAT 207..216
FT /note="2"
FT REPEAT 217..226
FT /note="3"
FT REPEAT 227..236
FT /note="4"
FT REPEAT 237..246
FT /note="5"
FT REPEAT 247..256
FT /note="6"
FT REPEAT 257..266
FT /note="7"
FT REPEAT 267..276
FT /note="8"
FT REPEAT 277..286
FT /note="9"
FT REPEAT 287..296
FT /note="10"
FT REPEAT 297..306
FT /note="11"
FT REPEAT 307..316
FT /note="12"
FT REPEAT 317..326
FT /note="13"
FT REPEAT 327..336
FT /note="14"
FT REPEAT 337..346
FT /note="15"
FT REPEAT 347..356
FT /note="16"
FT REPEAT 357..366
FT /note="17"
FT REPEAT 367..376
FT /note="18"
FT REPEAT 377..386
FT /note="19"
FT REPEAT 387..396
FT /note="20"
FT REPEAT 397..406
FT /note="21"
FT REPEAT 407..416
FT /note="22"
FT REPEAT 417..426
FT /note="23"
FT REPEAT 427..436
FT /note="24"
FT REPEAT 437..446
FT /note="25"
FT REPEAT 447..456
FT /note="26"
FT REPEAT 457..466
FT /note="27"
FT REPEAT 467..476
FT /note="28"
FT REPEAT 477..486
FT /note="29"
FT REPEAT 487..496
FT /note="30"
FT REPEAT 497..506
FT /note="31"
FT REPEAT 507..516
FT /note="32"
FT REPEAT 517..526
FT /note="33"
FT REPEAT 527..536
FT /note="34"
FT REPEAT 537..546
FT /note="35"
FT REPEAT 547..556
FT /note="36"
FT REPEAT 557..566
FT /note="37"
FT REPEAT 567..576
FT /note="38"
FT REPEAT 577..586
FT /note="39"
FT REPEAT 587..596
FT /note="40"
FT REPEAT 597..606
FT /note="41"
FT REPEAT 607..616
FT /note="42"
FT REPEAT 617..626
FT /note="43"
FT REPEAT 627..636
FT /note="44"
FT REPEAT 637..646
FT /note="45"
FT REPEAT 647..656
FT /note="46"
FT REPEAT 657..666
FT /note="47"
FT REPEAT 667..676
FT /note="48"
FT REPEAT 677..686
FT /note="49"
FT REPEAT 687..696
FT /note="50"
FT REPEAT 697..706
FT /note="51"
FT REPEAT 707..716
FT /note="52"
FT REPEAT 717..726
FT /note="53"
FT REPEAT 727..736
FT /note="54"
FT REGION 45..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..736
FT /note="54 X 10 AA tandem repeats of [NASG]-[QL]-[GS]-[KRT]-
FT [KR]-[AVTSEG]-[ED]-[AGVLS]-[ATGSV]-[PQLSA]"
FT REGION 968..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PL5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PL5"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT MOD_RES 1064
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99PL5"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2E9"
SQ SEQUENCE 1534 AA; 164586 MW; B343BCF12656F3C5 CRC64;
MDIYDTQTLG VMVFGGFMVV SAIGIFLVST FSMKETSYEE ALANQRKEMA KTHHQKVEKK
KKEKTVEKKG KTKKKEEKPN GKIPDHEPAP NVTILLKDPV RAPAVPVAPT PVQPPVVIAP
VATVPAMPQE KLAPSPKDKK KKEKKVAKVE PAVSSVVNSV QVLASKAAIL ETAPKEVPMV
VVPPVGAKAG TPATSTAQGK KAEGAQNQSR KAEGAPNQGK KAEGALNQGK KAEGAQNQGK
KVEVAPNQGK KAEGGQNQGK KVEGAQNQGK KAEGTPNQGK KAEGAPNQGK KTDGAPNQGK
KSEGAPNQGK KAEGAQNQGK KVEVAPNQGK KAEGGQNQGK KVEGAQNQGK KAEGTPNQGK
KAEGAPNQGK KTDGAPNQGK KSEGAPNQGK KVEGAQNQGK KVEGVQNQGK KAEGAQNQGK
KAEGTSSQGR KEEGTPNLGK KAEGSPNQGK KVEVVQNQSK KVEGAPNQGK KAEGSQNQGK
KTEGASNQGK KVDGAQNQGK KAEGAPNQGK KVEGAQNQGK KAEGTPNQGK KAEGAQNQGK
KAEGAPNQGK KAEGAPNQGK KAEGAPNQGK KAEGAPNQGK KAEAAPNQGK KAEGAPNQGK
KAEGAPNQGK KAEAAPNQGK KAEGAPNQGK KAEGAPNQGK KAEGAPNQGK KAEGAQNQGK
KAEGAPNQGK KADLVANQGT KAEGVAGQGK KAEGAPNQGK KGEGTPNQGK KSEGSPNQGK
KVDASANQSK RAESAPIQGK NADMVQSQEA PKQEAPAKKK SGSKKKGEPG PPDSDSPLYL
PYKTLVSTVG SMVFNEGEAQ RLIEILSEKA GVIQDTWHKA TQKGDPVAIL KRQLEEKEKL
LATEQEDAAV AKSKLREVNK ELAAEKAKAA AGEAKVKKQL VAREQEITAV QARIEASYRE
HVKEVQQLQG KIRTLQEQLE NGPNTQLARL QQENSILRDA LNQATSQVES KQNTELAKLR
QELSKVSKEL VEKSEAARQE EQQRKALETK TAALEKQVLQ LQASHKESEE ALQKRLDEVS
RELCRSQTSH ASLRADAEKA QEQQQQMAEL HSKLQSSEAE VKSKSEELSG LHGQLKEARA
ENSQLMERIR SIEALLEAGQ ARDTQDAQAS RAEHQARLKE LESQVWCLEK EATELKEAVE
QQKVKNNDLR EKNWKAMEAL ASAERACEEK LRSLTQAKEE SEKQLSLTEA QTKEALLALL
PALSSSAPQS YTEWLQELRE KGPELLKQRP ADTDPSSDLA SKLREAEETQ NNLQAECDQY
RTILAETEGM LKDLQKSVEE EEQVWKAKVS ATEEELQKSR VTVKHLEDIV EKLKGELESS
EQVREHTSHL EAELEKHMAA ASAECQSYAK EVAGLRQLLL ESQSQLDAAK SEAQKQSNEL
ALVRQQLSEM KSHVEDGDVA GSPAAPPAEQ DPVELKAQLE RTEATLEDEQ ALRRKLTAEF
QEAQSSACRL QAELEKLRST GPLESSAAEE ATQLKERLEK EKKLTSDLGH AATKLQELLK
TTQEQLAKER DTVKKLQEQL DKTDDSSSKE GTSV
