S23IP_HUMAN
ID S23IP_HUMAN Reviewed; 1000 AA.
AC Q9Y6Y8; D3DRD2; Q8IXH5; Q9BUK5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=SEC23-interacting protein;
DE AltName: Full=p125;
GN Name=SEC23IP; ORFNames=MSTP053;
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 [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 320-324;
RP 348-361; 397-410; 477-484; 591-596; 684-693; 695-700; 825-831; 853-866;
RP 871-877 AND 985-997, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH SEC23A.
RC TISSUE=Brain;
RX PubMed=10400679; DOI=10.1074/jbc.274.29.20505;
RA Tani K., Mizoguchi T., Iwamatsu A., Hatsuzawa K., Tagaya M.;
RT "p125 is a novel mammalian Sec23p-interacting protein with structural
RT similarity to phospholipid-modifying proteins.";
RL J. Biol. Chem. 274:20505-20512(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-644.
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y.,
RA Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-644.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-487.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP LACK OF ENZYME ACTIVITY.
RX PubMed=11788596; DOI=10.1074/jbc.m111092200;
RA Nakajima K., Sonoda H., Mizoguchi T., Aoki J., Arai H., Nagahama M.,
RA Tagaya M., Tani K.;
RT "A novel phospholipase A1 with sequence homology to a mammalian Sec23p-
RT interacting protein, p125.";
RL J. Biol. Chem. 277:11329-11335(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15623529; DOI=10.1074/jbc.m409673200;
RA Shimoi W., Ezawa I., Nakamoto K., Uesaki S., Gabreski G., Aridor M.,
RA Yamamoto A., Nagahama M., Tagaya M., Tani K.;
RT "p125 is localized in endoplasmic reticulum exit sites and involved in
RT their organization.";
RL J. Biol. Chem. 280:10141-10148(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, AND PHOSPHOLIPID-BINDING.
RX PubMed=22922100; DOI=10.1016/j.bbamcr.2012.02.002;
RA Inoue H., Baba T., Sato S., Ohtsuki R., Takemori A., Watanabe T.,
RA Tagaya M., Tani K.;
RT "Roles of SAM and DDHD domains in mammalian intracellular phospholipase A1
RT KIAA0725p.";
RL Biochim. Biophys. Acta 1823:930-939(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Plays a role in the organization of endoplasmic reticulum
CC exit sites. Specifically binds to phosphatidylinositol 3-phosphate
CC (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and
CC phosphatidylinositol 5-phosphate (PI(5)P).
CC {ECO:0000269|PubMed:10400679, ECO:0000269|PubMed:15623529,
CC ECO:0000269|PubMed:22922100}.
CC -!- SUBUNIT: Interacts with SEC23A. {ECO:0000269|PubMed:10400679}.
CC -!- INTERACTION:
CC Q9Y6Y8; Q9Y547: HSPB11; NbExp=3; IntAct=EBI-1767971, EBI-747101;
CC Q9Y6Y8; Q15436: SEC23A; NbExp=3; IntAct=EBI-1767971, EBI-81088;
CC Q9Y6Y8; A1L4H1: SSC5D; NbExp=6; IntAct=EBI-1767971, EBI-10172867;
CC Q9Y6Y8; O95070: YIF1A; NbExp=3; IntAct=EBI-1767971, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic
CC reticulum {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6Y8-2; Sequence=VSP_011831, VSP_011832;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with stronger levels
CC detected in heart, liver and skeletal muscle.
CC {ECO:0000269|PubMed:10400679}.
CC -!- SIMILARITY: Belongs to the PA-PLA1 family. {ECO:0000305}.
CC -!- CAUTION: Although belonging to the PA-PL1 family, does not seem to have
CC any phospholipase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP35401.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB019435; BAA77392.1; -; mRNA.
DR EMBL; AF116723; AAO15299.1; -; mRNA.
DR EMBL; CH471066; EAW49372.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49373.1; -; Genomic_DNA.
DR EMBL; BC063800; AAH63800.1; -; mRNA.
DR EMBL; BT006755; AAP35401.1; ALT_FRAME; mRNA.
DR CCDS; CCDS7618.1; -. [Q9Y6Y8-1]
DR RefSeq; NP_009121.1; NM_007190.3. [Q9Y6Y8-1]
DR AlphaFoldDB; Q9Y6Y8; -.
DR SMR; Q9Y6Y8; -.
DR BioGRID; 116365; 185.
DR CORUM; Q9Y6Y8; -.
DR IntAct; Q9Y6Y8; 36.
DR MINT; Q9Y6Y8; -.
DR STRING; 9606.ENSP00000358071; -.
DR SwissLipids; SLP:000001071; -.
DR GlyGen; Q9Y6Y8; 22 sites, 2 O-linked glycans (22 sites).
DR iPTMnet; Q9Y6Y8; -.
DR MetOSite; Q9Y6Y8; -.
DR PhosphoSitePlus; Q9Y6Y8; -.
DR BioMuta; SEC23IP; -.
DR DMDM; 55584014; -.
DR EPD; Q9Y6Y8; -.
DR jPOST; Q9Y6Y8; -.
DR MassIVE; Q9Y6Y8; -.
DR MaxQB; Q9Y6Y8; -.
DR PaxDb; Q9Y6Y8; -.
DR PeptideAtlas; Q9Y6Y8; -.
DR PRIDE; Q9Y6Y8; -.
DR ProteomicsDB; 86828; -. [Q9Y6Y8-1]
DR ProteomicsDB; 86829; -. [Q9Y6Y8-2]
DR Antibodypedia; 32172; 202 antibodies from 25 providers.
DR DNASU; 11196; -.
DR Ensembl; ENST00000369075.8; ENSP00000358071.3; ENSG00000107651.14. [Q9Y6Y8-1]
DR GeneID; 11196; -.
DR KEGG; hsa:11196; -.
DR MANE-Select; ENST00000369075.8; ENSP00000358071.3; NM_007190.4; NP_009121.1.
DR UCSC; uc001leu.3; human. [Q9Y6Y8-1]
DR CTD; 11196; -.
DR DisGeNET; 11196; -.
DR GeneCards; SEC23IP; -.
DR HGNC; HGNC:17018; SEC23IP.
DR HPA; ENSG00000107651; Low tissue specificity.
DR MIM; 617852; gene.
DR neXtProt; NX_Q9Y6Y8; -.
DR OpenTargets; ENSG00000107651; -.
DR PharmGKB; PA134964657; -.
DR VEuPathDB; HostDB:ENSG00000107651; -.
DR eggNOG; KOG2308; Eukaryota.
DR GeneTree; ENSGT00940000156602; -.
DR HOGENOM; CLU_006932_4_0_1; -.
DR InParanoid; Q9Y6Y8; -.
DR OMA; IRKAVYW; -.
DR OrthoDB; 777968at2759; -.
DR PhylomeDB; Q9Y6Y8; -.
DR TreeFam; TF314133; -.
DR PathwayCommons; Q9Y6Y8; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR SignaLink; Q9Y6Y8; -.
DR SIGNOR; Q9Y6Y8; -.
DR BioGRID-ORCS; 11196; 35 hits in 1076 CRISPR screens.
DR ChiTaRS; SEC23IP; human.
DR GeneWiki; SEC23IP; -.
DR GenomeRNAi; 11196; -.
DR Pharos; Q9Y6Y8; Tbio.
DR PRO; PR:Q9Y6Y8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9Y6Y8; protein.
DR Bgee; ENSG00000107651; Expressed in colonic epithelium and 201 other tissues.
DR ExpressionAtlas; Q9Y6Y8; baseline and differential.
DR Genevisible; Q9Y6Y8; HS.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; TAS:ProtInc.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR CDD; cd09584; SAM_sec23ip; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR004177; DDHD_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037603; SEC23IP_SAM.
DR Pfam; PF02862; DDHD; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM01127; DDHD; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1000
FT /note="SEC23-interacting protein"
FT /id="PRO_0000097554"
FT DOMAIN 644..707
FT /note="SAM"
FT DOMAIN 779..989
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 1..367
FT /note="Interaction with SEC23A"
FT /evidence="ECO:0000269|PubMed:10400679"
FT REGION 133..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZC7"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 920..924
FT /note="AEKVV -> GKFDI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011831"
FT VAR_SEQ 925..1000
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011832"
FT VARIANT 644
FT /note="K -> E (in dbSNP:rs2475298)"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT /id="VAR_019806"
FT CONFLICT 590
FT /note="F -> L (in Ref. 2; AAO15299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1000 AA; 111076 MW; DC71C274179F2CE9 CRC64;
MAERKPNGGS GGASTSSSGT NLLFSSSATE FSFNVPFIPV TQASASPASL LLPGEDSTDV
GEEDSFLGQT SIHTSAPQTF SYFSQVSSSS DPFGNIGQSP LTTAATSVGQ SGFPKPLTAL
PFTTGSQDVS NAFSPSISKA QPGAPPSSLM GINSYLPSQP SSLPPSYFGN QPQGIPQPGY
NPYRHTPGSS RANPYIAPPQ LQQCQTPGPP AHPPPSGPPV QMYQMPPGSL PPVPSSVQSP
AQQQVPARPG APSVQVPSPF LLQNQYEPVQ PHWFYCKEVE YKQLWMPFSV FDSLNLEEIY
NSVQPDPESV VLGTDGGRYD VYLYDRIRKA AYWEEEPAEV RRCTWFYKGD TDSRFIPYTE
EFSEKLEAEY KKAVTTNQWH RRLEFPSGET IVMHNPKVIV QFQPSSVPDE WGTTQDGQTR
PRVVKRGIDD NLDEIPDGEM PQVDHLVFVV HGIGPVCDLR FRSIIECVDD FRVVSLKLLR
THFKKSLDDG KVSRVEFLPV HWHSSLGGDA TGVDRNIKKI TLPSIGRFRH FTNETLLDIL
FYNSPTYCQT IVEKVGMEIN HLHALFMSRN PDFKGGVSVA GHSLGSLILF DILSNQKDLN
LSKCPGPLAV ANGVVKQLHF QEKQMPEEPK LTLDESYDLV VENKEVLTLQ ETLEALSLSE
YFSTFEKEKI DMESLLMCTV DDLKEMGIPL GPRKKIANFV EHKAAKLKKA ASEKKAVAAT
STKGQEQSAQ KTKDMASLPS ESNEPKRKLP VGACVSSVCV NYESFEVGAG QVSVAYNSLD
FEPEIFFALG SPIAMFLTIR GVDRIDENYS LPTCKGFFNI YHPLDPVAYR LEPMIVPDLD
LKAVLIPHHK GRKRLHLELK ESLSRMGSDL KQGFISSLKS AWQTLNEFAR AHTSSTQLQE
ELEKVANQIK EEEEKQVVEA EKVVESPDFS KDEDYLGKVG MLNGGRRIDY VLQEKPIESF
NEYLFALQSH LCYWESEDTA LLLLKEIYRT MNISPEQPQH
