SC16B_BOVIN
ID SC16B_BOVIN Reviewed; 1052 AA.
AC Q75NY9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Protein transport protein Sec16B;
DE AltName: Full=Regucalcin gene promoter region-related protein p117;
DE Short=RGPR-p117;
DE AltName: Full=SEC16 homolog B;
GN Name=SEC16B; Synonyms=RGPR;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=15583834;
RA Sawada N., Yamaguchi M.;
RT "A novel regucalcin gene promoter region-related protein: comparison of
RT nucleotide and amino acid sequences in vertebrate species.";
RL Int. J. Mol. Med. 15:97-104(2005).
CC -!- FUNCTION: Plays a role in the organization of the endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). Required for secretory cargo traffic from the endoplasmic
CC reticulum to the Golgi apparatus. Involved in peroxisome biogenesis.
CC Regulates the transport of peroxisomal biogenesis factors PEX3 and
CC PEX16 from the ER to peroxisomes. {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex. Interacts with TFG. Interacts with SEC13.
CC {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96JE7}; Peripheral membrane protein
CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Localizes to endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR EMBL; AB168116; BAD12777.2; -; mRNA.
DR RefSeq; NP_996854.2; NM_206971.2.
DR AlphaFoldDB; Q75NY9; -.
DR SMR; Q75NY9; -.
DR STRING; 9913.ENSBTAP00000001137; -.
DR PaxDb; Q75NY9; -.
DR PRIDE; Q75NY9; -.
DR GeneID; 404548; -.
DR KEGG; bta:404548; -.
DR CTD; 89866; -.
DR eggNOG; KOG1913; Eukaryota.
DR InParanoid; Q75NY9; -.
DR OrthoDB; 235062at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Peroxisome biogenesis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1052
FT /note="Protein transport protein Sec16B"
FT /id="PRO_0000341973"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..718
FT /note="Central conserved domain (CCD); required for
FT localization to endoplasmic reticulum exit sites"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT REGION 735..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N33"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N33"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
SQ SEQUENCE 1052 AA; 117174 MW; ED8DA79390CB163E CRC64;
MEPWIPQWLP QPSGRPPAPS KDPDRGLWKD RYYQPIPHSW HNGERVHQRQ DVGRSPQPQQ
DPREDLQEPH YAARSGEWRP PVSGVDYYEG GYPSQLYSRW SIEDLYQSYY SPALREEYAY
GSYYYHGHPQ QLQEERVPRQ GSPYIWQEDH RDQKYLNDHQ HENQNSPFGT NRETQLQSKS
RNPYKDSPAS NSGQERPEDL FMESPLTGAQ KNKLSLMEES NLLWQHESGL TSSSYELSQY
MADASELCDP MTSAVWSPVQ AEDISAAGPK EPMKFYVPHM PVSFGPGGQL VCVSPSSPSD
GQTALVELHS MEVILNDSEE QEEMRTFSGP LIREDVHKVD IMTFCQQKAA QSHKSETPGS
RDSALLWQLL VLLCRQNGSM VGSDIAELLM QDWKKLEKYK RQPPVANLIN LTDEDWPVLS
SGTRDLLTGE ILPSVETPAQ ILEKFTKLLY YGRKKEALEW AMKNHLWGHA LFLASKMDPR
THSRVMSGFT STLALNDPLQ TLFQLMSGRI PQAATCCGDK QWGDWRPHLA VILSNQGGDP
ELYQRTIVAM GDTLAGKGLV EAAHFCYLMA HVPFGYYTVK TDYLALLGSS HSQEFLKSAT
TEAIQRTEIF EYCQMLGRPK SFIPSFQVYK LLYASRLADY GLTSQALHYC EPVGTALLSH
GESSHPVLLV ELIKLAERLK LSDPLVLERR RHRGDRDLEP DWCVHLRGHH RELQQKEAGD
IGRPQSAQAV ISEARKTPEN TFYQDLSGPQ GNSEAYGDRS ALWPTLEQSG PAQLSPQQPR
SYPTGGGSGQ MGVPVPLYSV PETHLLGTSG SMAVTGAPGG TAWEEAQQIH LPPVSPETLQ
HPDGQKAISR PQVPLIPRAR SISESSIVSV KEDEEEPPRR QIKIFLKYRP ERKPEREGDT
KSSGFGWFSW FRSKPTHNAS PSGEEDSSDS PDSEEMPRAA SLPQPSPSLS LTPSPDPQSL
LGASAFSRDT GGDEVRGSVS GVGTAEGPGS GGLSGPEGVS TELCLNAGVL LPPPSVKGSV
PLYNPSQVPQ LSTVTSLNRP NRLAQRRYPT QS
