ID   YIPF3_RAT               Reviewed;         347 AA.
AC   Q6TUD4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein YIPF3;
DE   AltName: Full=Liver regeneration-related protein LRRGT00110;
DE   AltName: Full=YIP1 family member 3;
GN   Name=Yipf3;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA   Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B.,
RA   Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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).
CC   -!- FUNCTION: Involved in the maintenance of the Golgi structure. May play
CC       a role in hematopoiesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with YIPF4 and YIPF5.
CC       {ECO:0000250|UniProtKB:Q9GZM5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein. Golgi apparatus, cis-Golgi network membrane {ECO:0000250};
CC       Multi-pass membrane protein. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR   EMBL; AY387096; AAQ91066.1; -; mRNA.
DR   EMBL; BC087102; AAH87102.1; -; mRNA.
DR   RefSeq; NP_001007802.1; NM_001007801.2.
DR   AlphaFoldDB; Q6TUD4; -.
DR   BioGRID; 256888; 1.
DR   STRING; 10116.ENSRNOP00000025769; -.
DR   GlyGen; Q6TUD4; 1 site.
DR   jPOST; Q6TUD4; -.
DR   PaxDb; Q6TUD4; -.
DR   PRIDE; Q6TUD4; -.
DR   Ensembl; ENSRNOT00000025769; ENSRNOP00000025769; ENSRNOG00000018998.
DR   GeneID; 301245; -.
DR   KEGG; rno:301245; -.
DR   UCSC; RGD:1308185; rat.
DR   CTD; 25844; -.
DR   RGD; 1308185; Yipf3.
DR   eggNOG; KOG3114; Eukaryota.
DR   GeneTree; ENSGT00940000153766; -.
DR   HOGENOM; CLU_068070_0_0_1; -.
DR   InParanoid; Q6TUD4; -.
DR   OMA; HCIVLFV; -.
DR   OrthoDB; 1332379at2759; -.
DR   PhylomeDB; Q6TUD4; -.
DR   TreeFam; TF314073; -.
DR   PRO; PR:Q6TUD4; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000018998; Expressed in pancreas and 19 other tissues.
DR   Genevisible; Q6TUD4; RN.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR026637; YIPF3.
DR   PANTHER; PTHR15627:SF14; PTHR15627:SF14; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cytoplasm; Differentiation; Glycoprotein;
KW   Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZM5"
FT   CHAIN           2..347
FT                   /note="Protein YIPF3"
FT                   /id="PRO_0000244448"
FT   TOPO_DOM        2..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZM5"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..184
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..211
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        212..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..237
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        238..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..347
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZM5"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZM5"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   347 AA;  37973 MW;  1B010DCAFA14C9E1 CRC64;
     MATQAAPASG VRNGAGPEWG GFEENIQGGG SAVIDMENMD DTSGSSFEDM GELHQRLREE
     EVDADAAAAE EEDGEFLGMK GFKGQLSRQV ADQMWQAGKR QASKAFSLYA NIDILRPYFD
     VEPAQVRSRL LESMIPIKMV NFPQKVAGEL YGPLMLVFTL VAILLHGMKT SDTIIREGTL
     MGTAIGTCFG YWLGVSSFIY FLAYLCNAQI TMLQMLALLG YGLFGHCIVL FITYNIHLHA
     LFYLFWLLLG GLSTLRMVAV LVSRTVGPTQ RLLLCGTLAA LHMLFLLYLH FAYHKVVEGI
     LDTLEGPNIP PMQRVPRDIP AVLPAAKLPV AVVNATAKAI AVTLQSH