AP1B1_RAT
ID AP1B1_RAT Reviewed; 949 AA.
AC P52303;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=AP-1 complex subunit beta-1;
DE AltName: Full=Adaptor protein complex AP-1 subunit beta-1;
DE AltName: Full=Adaptor-related protein complex 1 subunit beta-1;
DE AltName: Full=Beta-1-adaptin;
DE AltName: Full=Beta-adaptin 1;
DE AltName: Full=Clathrin assembly protein complex 1 beta large chain;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin beta subunit;
GN Name=Ap1b1; Synonyms=Adtb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=2495531; DOI=10.1073/pnas.86.8.2612;
RA Kirchhausen T., Nathanson K.L., Matsui W., Vaisberg A., Chow E.P.,
RA Burne C., Keen J.H., Davis A.E.;
RT "Structural and functional division into two domains of the large (100- to
RT 115-kDa) chains of the clathrin-associated protein complex AP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2612-2616(1989).
RN [2]
RP CHARACTERIZATION OF ISOFORMS A AND B.
RX PubMed=7987321; DOI=10.1093/hmg/3.8.1393;
RA Peyrard M., Fransson I., Xie Y.-G., Han F.-Y., Ruttledge M.H., Swahn S.,
RA Collins J.E., Dunham I., Collins V.P., Dumanski J.P.;
RT "Characterization of a new member of the human beta-adaptin gene family
RT from chromosome 22q12, a candidate meningioma gene.";
RL Hum. Mol. Genet. 3:1393-1399(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-584, AND SUBUNIT.
RX PubMed=15377783; DOI=10.1073/pnas.0406102101;
RA Heldwein E.E., Macia E., Wang J., Yin H.L., Kirchhausen T., Harrison S.C.;
RT "Crystal structure of the clathrin adaptor protein 1 core.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14108-14113(2004).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC of clathrin to membranes and the recognition of sorting signals within
CC the cytosolic tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).
CC {ECO:0000269|PubMed:15377783}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P52303-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P52303-2; Sequence=VSP_000164;
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be part of the complex AP-2.
CC {ECO:0000305|PubMed:2495531}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77245; AAA40807.1; -; mRNA.
DR PIR; B32105; B32105.
DR RefSeq; NP_058973.1; NM_017277.1.
DR PDB; 1W63; X-ray; 4.00 A; B/D/F/H/J/L=1-584.
DR PDBsum; 1W63; -.
DR AlphaFoldDB; P52303; -.
DR SMR; P52303; -.
DR BioGRID; 248285; 5.
DR CORUM; P52303; -.
DR IntAct; P52303; 4.
DR MINT; P52303; -.
DR STRING; 10116.ENSRNOP00000054218; -.
DR iPTMnet; P52303; -.
DR PhosphoSitePlus; P52303; -.
DR SwissPalm; P52303; -.
DR jPOST; P52303; -.
DR PaxDb; P52303; -.
DR PRIDE; P52303; -.
DR GeneID; 29663; -.
DR UCSC; RGD:2064; rat. [P52303-1]
DR CTD; 162; -.
DR RGD; 2064; Ap1b1.
DR eggNOG; KOG1061; Eukaryota.
DR InParanoid; P52303; -.
DR PhylomeDB; P52303; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR EvolutionaryTrace; P52303; -.
DR PRO; PR:P52303; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030118; C:clathrin coat; IC:BHF-UCL.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030276; F:clathrin binding; IC:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0048268; P:clathrin coat assembly; IDA:BHF-UCL.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1150; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Direct protein sequencing; Golgi apparatus; Membrane; Nitration;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..949
FT /note="AP-1 complex subunit beta-1"
FT /id="PRO_0000193740"
FT REGION 592..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q10567"
FT MOD_RES 574
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35643"
FT VAR_SEQ 667..673
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000164"
SQ SEQUENCE 949 AA; 104589 MW; CC5AE54E8AACCD44 CRC64;
MTDSKYFTTT KKGEIFELKA ELNSDKKEKK KEAVKKVIAS MTVGKDVSAL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQLVEDQG FLDTLKDLIS DSNPMVVANR
VAALSEIAES HPSSNLLDLK AQSINKLLTA LNECTEWAQI FILDCLGNYM PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFMEML SKDLDYYATL LKKLAPPLVT LLSAEPEPQY
VPLRNINLIV QKRPEILKHE MKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIKDIFRK
YPNKYESVIA TLCENLDSLD EPEARAAMIW IVGEYAERID NADELLESFL DGFHDESTQV
QLQLLTAIVK LFLKKPTETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVAAKEV
VLAEKPLISE ETDLIEPTLL DELICYIGTL ASVYHKPPNA FVEGGRGVVH KSLPPRTASS
ESTESPEAAP AGAPASDQPD VIPAQGDLLG DLLNLDLGPP VSGPPLAASS VQMGAVDLLG
GGLDSLMGDE PEGIGDSNFG APPASVAAAA PARLGAPVSS GLSDLFDLTS GVGTLSGSYV
APKAVWLPAM KAKGLEISGT FTRQVGSISM DLQLTNKALQ VMTDFAIQFN RNSFGLAPAA
PLQVHAPLSP NQTVEISLPL NTVGSVMKME PLNNLQVAVK NNIDVFYFST LYPLHVLFVE
DGKMDRQMFL ATWKDIPNEN EAQFQIRDCP LNTEAASSKL QSSNIFTVAK RTVEGQDMLY
QSLKLTNGIW VLAELRIQPG NPSFTLSLKC RAPEVSQHDI QAYETILKN
