Full text data of SEC23IP
SEC23IP
[Confidence: low (only semi-automatic identification from reviews)]
SEC23-interacting protein (p125)
SEC23-interacting protein (p125)
UniProt
Q9Y6Y8
ID S23IP_HUMAN Reviewed; 1000 AA.
AC Q9Y6Y8; D3DRD2; Q8IXH5; Q9BUK5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 107.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
RP 853-866; 871-877 AND 985-997, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, 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
RP GLU-644.
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L.,
RA Zhao Y., Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L.,
RA Wu Q.Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT 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
RT Sec23p-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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RT phospholipase A1 KIAA0725p.";
RL Biochim. Biophys. Acta 1823:930-939(2012).
CC -!- FUNCTION: Plays a role in the organization of endoplasmic
CC reticulum exit sites. Specifically binds to phosphatidylinositol
CC 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P)
CC and phosphatidylinositol 5-phosphate (PI(5)P).
CC -!- SUBUNIT: Interacts with SEC23A.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side.
CC Endoplasmic reticulum (Probable).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with stronger levels
CC detected in heart, liver and skeletal muscle.
CC -!- SIMILARITY: Belongs to the PA-PLA1 family.
CC -!- SIMILARITY: Contains 1 DDHD domain.
CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC -!- CAUTION: Although belonging to the PA-PL1 family, does not seem to
CC have any phospholipase activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP35401.1; Type=Frameshift; Positions=471;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_009121.1; NM_007190.3.
DR UniGene; Hs.435004; -.
DR ProteinModelPortal; Q9Y6Y8; -.
DR SMR; Q9Y6Y8; 645-709.
DR IntAct; Q9Y6Y8; 1.
DR MINT; MINT-4999179; -.
DR STRING; 9606.ENSP00000358071; -.
DR PhosphoSite; Q9Y6Y8; -.
DR DMDM; 55584014; -.
DR PaxDb; Q9Y6Y8; -.
DR PRIDE; Q9Y6Y8; -.
DR DNASU; 11196; -.
DR Ensembl; ENST00000369075; ENSP00000358071; ENSG00000107651.
DR GeneID; 11196; -.
DR KEGG; hsa:11196; -.
DR UCSC; uc001leu.2; human.
DR CTD; 11196; -.
DR GeneCards; GC10P121642; -.
DR HGNC; HGNC:17018; SEC23IP.
DR HPA; HPA038403; -.
DR neXtProt; NX_Q9Y6Y8; -.
DR PharmGKB; PA134964657; -.
DR eggNOG; NOG285690; -.
DR HOGENOM; HOG000007725; -.
DR HOVERGEN; HBG057256; -.
DR InParanoid; Q9Y6Y8; -.
DR OMA; EIFFALG; -.
DR OrthoDB; EOG7JDQWX; -.
DR PhylomeDB; Q9Y6Y8; -.
DR ChiTaRS; SEC23IP; human.
DR GeneWiki; SEC23IP; -.
DR GenomeRNAi; 11196; -.
DR NextBio; 42613; -.
DR PRO; PR:Q9Y6Y8; -.
DR ArrayExpress; Q9Y6Y8; -.
DR Bgee; Q9Y6Y8; -.
DR CleanEx; HS_SEC23IP; -.
DR Genevestigator; Q9Y6Y8; -.
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:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR004177; DDHD.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR021129; SAM_type1.
DR Pfam; PF02862; DDHD; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51043; DDHD; 1.
DR PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1000 SEC23-interacting protein.
FT /FTId=PRO_0000097554.
FT DOMAIN 644 707 SAM.
FT DOMAIN 779 989 DDHD.
FT REGION 1 367 Interaction with SEC23A.
FT COMPBIAS 142 259 Pro-rich.
FT MOD_RES 926 926 Phosphoserine.
FT VAR_SEQ 920 924 AEKVV -> GKFDI (in isoform 2).
FT /FTId=VSP_011831.
FT VAR_SEQ 925 1000 Missing (in isoform 2).
FT /FTId=VSP_011832.
FT VARIANT 644 644 K -> E (in dbSNP:rs2475298).
FT /FTId=VAR_019806.
FT CONFLICT 590 590 F -> L (in Ref. 2; AAO15299).
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
//
ID S23IP_HUMAN Reviewed; 1000 AA.
AC Q9Y6Y8; D3DRD2; Q8IXH5; Q9BUK5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 107.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
RP 853-866; 871-877 AND 985-997, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, 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
RP GLU-644.
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L.,
RA Zhao Y., Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L.,
RA Wu Q.Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT 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
RT Sec23p-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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RT phospholipase A1 KIAA0725p.";
RL Biochim. Biophys. Acta 1823:930-939(2012).
CC -!- FUNCTION: Plays a role in the organization of endoplasmic
CC reticulum exit sites. Specifically binds to phosphatidylinositol
CC 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P)
CC and phosphatidylinositol 5-phosphate (PI(5)P).
CC -!- SUBUNIT: Interacts with SEC23A.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side.
CC Endoplasmic reticulum (Probable).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with stronger levels
CC detected in heart, liver and skeletal muscle.
CC -!- SIMILARITY: Belongs to the PA-PLA1 family.
CC -!- SIMILARITY: Contains 1 DDHD domain.
CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC -!- CAUTION: Although belonging to the PA-PL1 family, does not seem to
CC have any phospholipase activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP35401.1; Type=Frameshift; Positions=471;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_009121.1; NM_007190.3.
DR UniGene; Hs.435004; -.
DR ProteinModelPortal; Q9Y6Y8; -.
DR SMR; Q9Y6Y8; 645-709.
DR IntAct; Q9Y6Y8; 1.
DR MINT; MINT-4999179; -.
DR STRING; 9606.ENSP00000358071; -.
DR PhosphoSite; Q9Y6Y8; -.
DR DMDM; 55584014; -.
DR PaxDb; Q9Y6Y8; -.
DR PRIDE; Q9Y6Y8; -.
DR DNASU; 11196; -.
DR Ensembl; ENST00000369075; ENSP00000358071; ENSG00000107651.
DR GeneID; 11196; -.
DR KEGG; hsa:11196; -.
DR UCSC; uc001leu.2; human.
DR CTD; 11196; -.
DR GeneCards; GC10P121642; -.
DR HGNC; HGNC:17018; SEC23IP.
DR HPA; HPA038403; -.
DR neXtProt; NX_Q9Y6Y8; -.
DR PharmGKB; PA134964657; -.
DR eggNOG; NOG285690; -.
DR HOGENOM; HOG000007725; -.
DR HOVERGEN; HBG057256; -.
DR InParanoid; Q9Y6Y8; -.
DR OMA; EIFFALG; -.
DR OrthoDB; EOG7JDQWX; -.
DR PhylomeDB; Q9Y6Y8; -.
DR ChiTaRS; SEC23IP; human.
DR GeneWiki; SEC23IP; -.
DR GenomeRNAi; 11196; -.
DR NextBio; 42613; -.
DR PRO; PR:Q9Y6Y8; -.
DR ArrayExpress; Q9Y6Y8; -.
DR Bgee; Q9Y6Y8; -.
DR CleanEx; HS_SEC23IP; -.
DR Genevestigator; Q9Y6Y8; -.
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:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR004177; DDHD.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR021129; SAM_type1.
DR Pfam; PF02862; DDHD; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51043; DDHD; 1.
DR PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1000 SEC23-interacting protein.
FT /FTId=PRO_0000097554.
FT DOMAIN 644 707 SAM.
FT DOMAIN 779 989 DDHD.
FT REGION 1 367 Interaction with SEC23A.
FT COMPBIAS 142 259 Pro-rich.
FT MOD_RES 926 926 Phosphoserine.
FT VAR_SEQ 920 924 AEKVV -> GKFDI (in isoform 2).
FT /FTId=VSP_011831.
FT VAR_SEQ 925 1000 Missing (in isoform 2).
FT /FTId=VSP_011832.
FT VARIANT 644 644 K -> E (in dbSNP:rs2475298).
FT /FTId=VAR_019806.
FT CONFLICT 590 590 F -> L (in Ref. 2; AAO15299).
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
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