ID   AP1B1_BOVIN             Reviewed;         951 AA.
AC   Q08DS7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=AP2B1;
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].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC       Note=Component of the coat surrounding the cytoplasmic face of coated
CC       vesicles located at the Golgi complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; BC123583; AAI23584.1; -; mRNA.
DR   RefSeq; NP_001068593.1; NM_001075125.1.
DR   RefSeq; XP_010814093.1; XM_010815791.2.
DR   RefSeq; XP_015323437.1; XM_015467951.1.
DR   AlphaFoldDB; Q08DS7; -.
DR   SMR; Q08DS7; -.
DR   BioGRID; 159457; 2.
DR   STRING; 9913.ENSBTAP00000027078; -.
DR   PaxDb; Q08DS7; -.
DR   PRIDE; Q08DS7; -.
DR   Ensembl; ENSBTAT00000076585; ENSBTAP00000060816; ENSBTAG00000020316.
DR   GeneID; 282183; -.
DR   KEGG; bta:282183; -.
DR   CTD; 163; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020316; -.
DR   VGNC; VGNC:55033; AP2B1.
DR   eggNOG; KOG1061; Eukaryota.
DR   GeneTree; ENSGT00940000155206; -.
DR   InParanoid; Q08DS7; -.
DR   OMA; ASIYHKS; -.
DR   OrthoDB; 323029at2759; -.
DR   Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000020316; Expressed in spermatid and 105 other tissues.
DR   ExpressionAtlas; Q08DS7; baseline and differential.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
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; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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; IPR000225; Armadillo.
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; SM00185; ARM; 2.
DR   SMART; SM01020; B2-adapt-app_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasmic vesicle; Golgi apparatus; Membrane; Nitration;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..951
FT                   /note="AP-1 complex subunit beta-1"
FT                   /id="PRO_0000283800"
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"
SQ   SEQUENCE   951 AA;  105706 MW;  3071B89A32674CA3 CRC64;
     MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT
     DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE
     YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA
     VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI
     CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKESDYYNML LKKLAPPLVT LLSGEPEVQY
     VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
     YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK
     YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
     QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV
     VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
     DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL
     DSLLGSDLGG GIGGSPAVGQ SFIPSSVPAT FAPSPTPAVV SSGLNDLFEL STGIGMAPGG
     YVAPKAVWLP AVKAKGLEIS GTFTHRQGHI YMEMNFTNKA LQHMTDFAIQ FNKNSFGVIP
     STPLAIHTPL MPNQSIDVSL PLNTLGPVMK MEPLNNLQVA VKNNIDVFYF SCLIPLNVLF
     VEDGKMERQV FLATWKDIPN ENELQFQIKE CHLNADTVSS KLQNNNVYTI AKRNVEGQDM
     LYQSLKLTNG IWILAELRIQ PGNPNYTLSL KCRAPEVSQY IYQVYDSILK N