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YIF1B_RAT
ID   YIF1B_RAT               Reviewed;         259 AA.
AC   Q6PEC3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Protein YIF1B;
DE   AltName: Full=YIP1-interacting factor homolog B;
GN   Name=Yif1b {ECO:0000312|RGD:735199};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 (ISOFORM 1).
RG   Amgen EST program;
RT   "Amgen rat EST program.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   TISSUE SPECIFICITY, INTERACTION WITH HTR1A, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RX   PubMed=18685031; DOI=10.1523/jneurosci.4487-07.2008;
RA   Carrel D., Masson J., Al Awabdh S., Capra C.B., Lenkei Z., Hamon M.,
RA   Emerit M.B., Darmon M.;
RT   "Targeting of the 5-HT1A serotonin receptor to neuronal dendrites is
RT   mediated by Yif1B.";
RL   J. Neurosci. 28:8063-8073(2008).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26077767; DOI=10.1111/tra.12306;
RA   Alterio J., Masson J., Diaz J., Chachlaki K., Salman H., Areias J.,
RA   Al Awabdh S., Emerit M.B., Darmon M.;
RT   "Yif1B Is Involved in the Anterograde Traffic Pathway and the Golgi
RT   Architecture.";
RL   Traffic 16:978-993(2015).
CC   -!- FUNCTION: Functions in endoplasmic reticulum to Golgi vesicle-mediated
CC       transport and regulates the proper organization of the endoplasmic
CC       reticulum and the Golgi (By similarity). Plays a key role in targeting
CC       to neuronal dendrites receptors such as HTR1A (PubMed:18685031). Plays
CC       also a role in primary cilium and sperm flagellum assembly probably
CC       through protein transport to these compartments (By similarity).
CC       {ECO:0000250|UniProtKB:Q9CX30, ECO:0000269|PubMed:18685031}.
CC   -!- SUBUNIT: Interacts with HTR1A (via C-terminus) (PubMed:18685031).
CC       Interacts with ABCB9 (via TMD0); this interaction allows (but is not
CC       essential) the ER-to-Golgi trafficking and strongly depends on a salt
CC       bridge within TMD0 (By similarity). {ECO:0000250|UniProtKB:Q5BJH7,
CC       ECO:0000269|PubMed:18685031}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26077767}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26077767};
CC       Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi
CC       intermediate compartment membrane {ECO:0000269|PubMed:18685031,
CC       ECO:0000269|PubMed:26077767}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Shuttles between the endoplasmic reticulum, the
CC       intermediate compartment and the Golgi apparatus.
CC       {ECO:0000269|PubMed:26077767}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PEC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PEC3-2; Sequence=VSP_028657;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed in heart,
CC       kidney, and lung and lower levels in spleen, muscle, and intestine (at
CC       protein level) (PubMed:18685031). Expressed in serotoninergic neurons
CC       (at protein level) (PubMed:18685031). {ECO:0000269|PubMed:18685031}.
CC   -!- SIMILARITY: Belongs to the YIF1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC058153; AAH58153.1; ALT_INIT; mRNA.
DR   EMBL; CB797587; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001014810.1; NM_001014810.1.
DR   RefSeq; NP_942029.2; NM_198734.2.
DR   AlphaFoldDB; Q6PEC3; -.
DR   IntAct; Q6PEC3; 2.
DR   MINT; Q6PEC3; -.
DR   PRIDE; Q6PEC3; -.
DR   Ensembl; ENSRNOT00000044145; ENSRNOP00000045414; ENSRNOG00000055286. [Q6PEC3-1]
DR   GeneID; 292768; -.
DR   KEGG; rno:292768; -.
DR   UCSC; RGD:735199; rat. [Q6PEC3-1]
DR   CTD; 90522; -.
DR   RGD; 735199; Yif1b.
DR   GeneTree; ENSGT00390000009423; -.
DR   HOGENOM; CLU_047877_1_1_1; -.
DR   InParanoid; Q6PEC3; -.
DR   OrthoDB; 1256839at2759; -.
DR   PhylomeDB; Q6PEC3; -.
DR   PRO; PR:Q6PEC3; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020616; Expressed in thymus and 19 other tissues.
DR   ExpressionAtlas; Q6PEC3; baseline.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR   GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0120316; P:sperm flagellum assembly; ISS:UniProtKB.
DR   InterPro; IPR005578; Yif1_fam.
DR   PANTHER; PTHR14083; PTHR14083; 2.
DR   Pfam; PF03878; YIF1; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Endoplasmic reticulum; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..259
FT                   /note="Protein YIF1B"
FT                   /id="PRO_0000307260"
FT   TOPO_DOM        9..153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CX30"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CX30"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BJH7"
FT   VAR_SEQ         1..19
FT                   /note="MHATGLAAPAGTPRLRKWP -> MPRPGRGRIAA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028657"
SQ   SEQUENCE   259 AA;  28418 MW;  C918AA2E90B9B204 CRC64;
     MHATGLAAPA GTPRLRKWPS KRRVPVSQPG MADPHQFFDD TSSAPSRGYG GQPSPGSLGY
     PTSSSEAAFL AAPMSNMAMA YGSSLAAQGK ELVDKNIDRF IPVSKLKYYF AVDTVYVGKK
     LGLLVFPYLH QDWEVQYQQD TPVAPRFDIN APDLYIPAMA FITYILVAGL ALGTQDRMIG
     GVLTGLLFGK IGYYLVLAWC CVSIFVFMIR TLRLKILAQA AAEGVPVRGA RNQLRMYLTM
     AVAAAQPVLM YWLTFHLVR
 
 
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