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YIPF2_HUMAN
ID   YIPF2_HUMAN             Reviewed;         316 AA.
AC   Q9BWQ6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Protein YIPF2;
DE   AltName: Full=YIP1 family member 2;
GN   Name=YIPF2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Renal cell carcinoma, and Rhabdomyosarcoma;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH YIPF1 AND YIPF6.
RX   PubMed=28286305; DOI=10.1016/j.yexcr.2017.03.011;
RA   Soonthornsit J., Sakai N., Sasaki Y., Watanabe R., Osako S., Nakamura N.;
RT   "YIPF1, YIPF2, and YIPF6 are medial-/trans-Golgi and trans-Golgi network-
RT   localized Yip domain family proteins, which play a role in the Golgi
RT   reassembly and glycan synthesis.";
RL   Exp. Cell Res. 353:100-108(2017).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=27999994; DOI=10.1007/s00418-016-1527-3;
RA   Kranjc T., Dempsey E., Cagney G., Nakamura N., Shields D.C., Simpson J.C.;
RT   "Functional characterisation of the YIPF protein family in mammalian
RT   cells.";
RL   Histochem. Cell Biol. 147:439-451(2017).
CC   -!- SUBUNIT: Interacts with YIPF6; this interaction may stabilize YIPF2.
CC       May also form a ternary complex with YIPF1 and YIPF6.
CC       {ECO:0000269|PubMed:28286305}.
CC   -!- INTERACTION:
CC       Q9BWQ6; Q13520: AQP6; NbExp=3; IntAct=EBI-751204, EBI-13059134;
CC       Q9BWQ6; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-751204, EBI-781551;
CC       Q9BWQ6; O15552: FFAR2; NbExp=3; IntAct=EBI-751204, EBI-2833872;
CC       Q9BWQ6; O15529: GPR42; NbExp=3; IntAct=EBI-751204, EBI-18076404;
CC       Q9BWQ6; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-751204, EBI-18053395;
CC       Q9BWQ6; O95214: LEPROTL1; NbExp=3; IntAct=EBI-751204, EBI-750776;
CC       Q9BWQ6; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-751204, EBI-373355;
CC       Q9BWQ6; O15173: PGRMC2; NbExp=3; IntAct=EBI-751204, EBI-1050125;
CC       Q9BWQ6; Q96GF1: RNF185; NbExp=6; IntAct=EBI-751204, EBI-2340249;
CC       Q9BWQ6; Q99942: RNF5; NbExp=6; IntAct=EBI-751204, EBI-348482;
CC       Q9BWQ6; Q6UWV7: SHISAL2A; NbExp=3; IntAct=EBI-751204, EBI-18396772;
CC       Q9BWQ6; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-751204, EBI-18159983;
CC       Q9BWQ6; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-751204, EBI-8644112;
CC       Q9BWQ6; Q9BRY0-2: SLC39A3; NbExp=3; IntAct=EBI-751204, EBI-17714201;
CC       Q9BWQ6; Q86WV6: STING1; NbExp=3; IntAct=EBI-751204, EBI-2800345;
CC       Q9BWQ6; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-751204, EBI-18196631;
CC       Q9BWQ6; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-751204, EBI-13342951;
CC       Q9BWQ6; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-751204, EBI-8638294;
CC       Q9BWQ6; Q9Y320: TMX2; NbExp=3; IntAct=EBI-751204, EBI-6447886;
CC       Q9BWQ6; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-751204, EBI-11343401;
CC       Q9BWQ6; Q96EC8: YIPF6; NbExp=9; IntAct=EBI-751204, EBI-751210;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000269|PubMed:27999994}; Multi-pass membrane protein
CC       {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:27999994}. Late endosome membrane
CC       {ECO:0000269|PubMed:27999994}. Note=Mainly localizes within
CC       medial-/trans-Golgi and trans-Golgi network (TGN), while less so within
CC       cis-Golgi. {ECO:0000269|PubMed:27999994, ECO:0000269|PubMed:28286305}.
CC   -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR   EMBL; BC000056; AAH00056.1; -; mRNA.
DR   EMBL; BC013014; AAH13014.1; -; mRNA.
DR   CCDS; CCDS12251.1; -.
DR   RefSeq; NP_001308368.1; NM_001321439.1.
DR   RefSeq; NP_076934.1; NM_024029.4.
DR   RefSeq; XP_011526572.1; XM_011528270.2.
DR   AlphaFoldDB; Q9BWQ6; -.
DR   BioGRID; 122463; 30.
DR   IntAct; Q9BWQ6; 26.
DR   MINT; Q9BWQ6; -.
DR   STRING; 9606.ENSP00000253031; -.
DR   TCDB; 9.B.135.2.7; the membrane trafficking yip (yip) family.
DR   iPTMnet; Q9BWQ6; -.
DR   PhosphoSitePlus; Q9BWQ6; -.
DR   BioMuta; YIPF2; -.
DR   DMDM; 74733454; -.
DR   EPD; Q9BWQ6; -.
DR   jPOST; Q9BWQ6; -.
DR   MassIVE; Q9BWQ6; -.
DR   MaxQB; Q9BWQ6; -.
DR   PaxDb; Q9BWQ6; -.
DR   PeptideAtlas; Q9BWQ6; -.
DR   PRIDE; Q9BWQ6; -.
DR   ProteomicsDB; 79304; -.
DR   Antibodypedia; 13058; 27 antibodies from 15 providers.
DR   DNASU; 78992; -.
DR   Ensembl; ENST00000253031.6; ENSP00000253031.1; ENSG00000130733.11.
DR   Ensembl; ENST00000586748.6; ENSP00000466055.1; ENSG00000130733.11.
DR   GeneID; 78992; -.
DR   KEGG; hsa:78992; -.
DR   MANE-Select; ENST00000586748.6; ENSP00000466055.1; NM_001321439.2; NP_001308368.1.
DR   UCSC; uc002mqb.4; human.
DR   CTD; 78992; -.
DR   DisGeNET; 78992; -.
DR   GeneCards; YIPF2; -.
DR   HGNC; HGNC:28476; YIPF2.
DR   HPA; ENSG00000130733; Low tissue specificity.
DR   MIM; 617522; gene.
DR   neXtProt; NX_Q9BWQ6; -.
DR   OpenTargets; ENSG00000130733; -.
DR   PharmGKB; PA142670556; -.
DR   VEuPathDB; HostDB:ENSG00000130733; -.
DR   eggNOG; KOG3114; Eukaryota.
DR   GeneTree; ENSGT00390000010157; -.
DR   InParanoid; Q9BWQ6; -.
DR   OMA; HYNFHLV; -.
DR   OrthoDB; 1425332at2759; -.
DR   PhylomeDB; Q9BWQ6; -.
DR   PathwayCommons; Q9BWQ6; -.
DR   SignaLink; Q9BWQ6; -.
DR   BioGRID-ORCS; 78992; 20 hits in 1080 CRISPR screens.
DR   ChiTaRS; YIPF2; human.
DR   GenomeRNAi; 78992; -.
DR   Pharos; Q9BWQ6; Tdark.
DR   PRO; PR:Q9BWQ6; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9BWQ6; protein.
DR   Bgee; ENSG00000130733; Expressed in type B pancreatic cell and 191 other tissues.
DR   ExpressionAtlas; Q9BWQ6; baseline and differential.
DR   Genevisible; Q9BWQ6; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB.
DR   GO; GO:0000138; C:Golgi trans cisterna; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR006977; Yip1_dom.
DR   InterPro; IPR039765; Yip5/YIPF1/YIPF2.
DR   PANTHER; PTHR12822; PTHR12822; 1.
DR   Pfam; PF04893; Yip1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endosome; Golgi apparatus; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..316
FT                   /note="Protein YIPF2"
FT                   /id="PRO_0000241454"
FT   TOPO_DOM        2..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27999994"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..163
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        197..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..231
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..316
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:27999994"
FT   REGION          16..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   316 AA;  35151 MW;  274E5F2D07EA1A75 CRC64;
     MASADELTFH EFEEATNLLA DTPDAATTSR SDQLTPQGHV AVAVGSGGSY GAEDEVEEES
     DKAALLQEQQ QQQQPGFWTF SYYQSFFDVD TSQVLDRIKG SLLPRPGHNF VRHHLRNRPD
     LYGPFWICAT LAFVLAVTGN LTLVLAQRRD PSIHYSPQFH KVTVAGISIY CYAWLVPLAL
     WGFLRWRKGV QERMGPYTFL ETVCIYGYSL FVFIPMVVLW LIPVPWLQWL FGALALGLSA
     AGLVFTLWPV VREDTRLVAT VLLSVVVLLH ALLAMGCKLY FFQSLPPENV APPPQITSLP
     SNIALSPTLP QSLAPS
 
 
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