ID   MIP2_ARATH              Reviewed;        2376 AA.
AC   Q9FIN7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=MAG2-interacting protein 2 {ECO:0000303|PubMed:24118572};
GN   Name=MIP2 {ECO:0000303|PubMed:24118572};
GN   OrderedLocusNames=At5g24350 {ECO:0000312|Araport:AT5G24350};
GN   ORFNames=K16H17.4 {ECO:0000312|EMBL:BAB11228.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAG2, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=24118572; DOI=10.1111/tpj.12347;
RA   Li L., Shimada T., Takahashi H., Koumoto Y., Shirakawa M., Takagi J.,
RA   Zhao X., Tu B., Jin H., Shen Z., Han B., Jia M., Kondo M., Nishimura M.,
RA   Hara-Nishimura I.;
RT   "MAG2 and three MAG2-INTERACTING PROTEINs form an ER-localized complex to
RT   facilitate storage protein transport in Arabidopsis thaliana.";
RL   Plant J. 76:781-791(2013).
CC   -!- FUNCTION: Required for proper maturation of seed storage proteins.
CC       Forms a complex with MAG2, ZW10/MIP1 and MIP3 on the endoplasmic
CC       reticulum that may be responsible for efficient transport of seed
CC       storage proteins. {ECO:0000269|PubMed:24118572}.
CC   -!- SUBUNIT: Forms a complex with MAG2, ZW10/MIP1 and MIP3 on the
CC       endoplasmic reticulum. {ECO:0000269|PubMed:24118572}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:24118572}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:24118572}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FIN7-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Accumulation of the precursors of the two major
CC       storage proteins albumin 2S and globulin 12S in dry seeds.
CC       {ECO:0000269|PubMed:24118572}.
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DR   EMBL; AB016884; BAB11228.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93296.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69227.1; -; Genomic_DNA.
DR   RefSeq; NP_001318636.1; NM_001343876.1. [Q9FIN7-1]
DR   RefSeq; NP_197823.1; NM_122343.3. [Q9FIN7-1]
DR   AlphaFoldDB; Q9FIN7; -.
DR   BioGRID; 17780; 3.
DR   STRING; 3702.AT5G24350.2; -.
DR   PaxDb; Q9FIN7; -.
DR   PRIDE; Q9FIN7; -.
DR   ProteomicsDB; 250707; -. [Q9FIN7-1]
DR   EnsemblPlants; AT5G24350.1; AT5G24350.1; AT5G24350. [Q9FIN7-1]
DR   EnsemblPlants; AT5G24350.3; AT5G24350.3; AT5G24350. [Q9FIN7-1]
DR   GeneID; 832505; -.
DR   Gramene; AT5G24350.1; AT5G24350.1; AT5G24350. [Q9FIN7-1]
DR   Gramene; AT5G24350.3; AT5G24350.3; AT5G24350. [Q9FIN7-1]
DR   KEGG; ath:AT5G24350; -.
DR   Araport; AT5G24350; -.
DR   eggNOG; KOG1797; Eukaryota.
DR   HOGENOM; CLU_001017_0_0_1; -.
DR   PhylomeDB; Q9FIN7; -.
DR   PRO; PR:Q9FIN7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIN7; baseline and differential.
DR   Genevisible; Q9FIN7; AT.
DR   GO; GO:0070939; C:Dsl1/NZR complex; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IEA:GOC.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0051604; P:protein maturation; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0006624; P:vacuolar protein processing; TAS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR013244; Sec39_domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF08314; Sec39; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..2376
FT                   /note="MAG2-interacting protein 2"
FT                   /id="PRO_0000430534"
SQ   SEQUENCE   2376 AA;  266814 MW;  266120288DAFCFB6 CRC64;
     MESPGRKVLY EIRHHASLPY VPRYPPLPQA DGTNSKGGLR SLVSIKGVSQ LKEKWSEYWN
     PKKTNKPVSL FISPRGELVA VTSGNHVTIL RKDDDYRKPC GNFTSSISGS FTSGVWSEKH
     DVLGLVDDSE TLFFIRANGE EISQVTKRNL KVSAPVLGLM EDDSDLQPSC LCSFSILTSD
     GRIHHVEISR EPSASAFSKH ASNSVSKQFP NHVFCFDYHP DLSFLLIVGS VAGISSSGSS
     GSSCISLWRK CQNLGLELLS TTKFDGVYCE NKDDQLAYPK TLISPQGSHV ASLDSNGCVH
     IFQLDKARLT LSCCPSEDSS DSLKPDKSLQ SWKESLRNVV DFTWWSDHAL AILKRSGNIS
     IFDISRCVIV QEDATIYSMP VVERVQKYEG HIFLLESSTQ EAKSALANVD RDASEFHHTS
     EHSMLWRLIS FTEKTIPEMY KILVEKCQYQ EALDFSDSHG LDRDEVFKSR WLKSEKGVSD
     VSTILSKIKD KAFVLSECLD RIGPTEDSMK ALLAHGLYLT NHYVFAKSED QESQQLWEFR
     LARLRLLQFS ERLDTYLGIS MGRYSVQDYR KFRSNPINQA AISLAESGRI GALNLLFKRH
     PYSLVSFMLQ ILAAIPETVP VETYAHLLPG KSPPTSMAVR EEDWVECEKM VKFINNLPEN
     GKNDSLIQTE PIVRRCLGYN WPSSEELAAW YKSRARDIDS TTGLLDNCIC LIDIACRKGI
     SELEQFHEDL SYLHQIIYSD EIGGEICFSL SLAGWEHLSD YEKFKIMLEG VKADTVVRRL
     HEKAIPFMQK RFLGTNNQNV ESFLVKWLKE MAAKSDMDLC SKVIDEGCID LYTVCFFKDD
     VEAVDCALQC LYLCKVTDKW NVMATMLSKL PKINDKAGED IQRRLKRAEG HIEAGRLLEF
     YQVPKPINYF LEVHLDEKGV KQILRLMLSK FVRRQPGRSD NDWACMWRDL RQLQEKAFYF
     LDLEFVLTEF CRGLLKAGKF SLARNYLKGT GSVALPSEKA ESLVINAAKE YFFSAPSLAS
     EEIWKARECL NIFSSSRTVK AEDDIIDAVT VRLPKLGVSL LPVQFKQVKD PMEIIKMAIT
     GDPEAYLHGE ELIEVAKLLG LNSSEDISSV KEAIAREAAI AGDMQLAFDL CLVLTKEGHG
     PIWDLGAAIA RSPALEHMDI SSRKQLLGFA LGHCDDESIS ELLHAWKDFD LQGQCETLGM
     LSESNSPEFQ KMDGVSCLTD FPQMLDGLSS DQQLDLDRAK DSISCVAKDM PVDDSVDLES
     LLKENGKLFS FAASHLPWLL KLGRNRKLDK SLVLDSIPGK QFVSIKATAL ITILSWLAKN
     GFAPKDELIA MITDSIIEHP VTKEEDVIGC SFLLNLVDAS NAVEVIEKQL RIRGNYQEIR
     SIMSLGMIYS LLHDSGVECT APIQRRELLQ KNFERKQTES LADDMSKIDK LQSTFWKEWK
     HKLEEKMHDA DRSRMLERII PGVETERFLS HDIEYIKVAV FSLIESVKSE KKLILKDVLK
     LADTYGLKQS EVILRYLSSI LCSEIWTNED ITAEILQVKE EILTFASDTI ETISTIVYPA
     ASGLNKQRLA YIYSLLSECY CHLAESKEAS LLVQPNSSFA GLSNWYNVLK QECSRVSFIK
     DLDFKNISEL GGLNFDSFNN EVHAHINEMN LEALAKMVET LSGLSMENSS KGLISCQDVY
     KQYIMNLLDT LESRRDLDFG SAESFQGFLG QLEKTYDHCR VYVRILEPLQ AVEILKRHFT
     LVLPPNGSYM HIPDSSTWQE CLILLINFWI RLADEMQEVK SSNPSLVENL TLSPECISSC
     FTLLIKLVMY DSLSPSQAWA AILVYLRSGL VGDCATEIFN FCRAMVFSGC GFGPISDVFS
     DMSSRYPTAL QDLPHLYLSV LEPILQDLVS GAPETQNLYR LLSSLSNLEG NLEELKRVRL
     VVWKQLVIFS ENLELPSQVR VYSLELMQFI SGKNIKGSSS ELQSNVMPWD GSAELLSSMQ
     KTEAALNQAL PDQADGSSRL TNTLVALKSS QVAVAAISPG LEISPEDLST VETSVSCFSK
     LSAAVTTASQ AEALLAILEG WEELFEAKNA ELLPSNEATD QGNDWGDDDW NDGWETLQES
     EPVEKVKKEC VVSAHPLHSC WLDIFRKYIA LSMPENVLQL IDGSLQKPEE VIIEETEAES
     LTGILARTDP FLALKISLLL PYKQIRSQCL SVVEEQLKQE GIPELSSQSH HEVLLLVIYS
     GTLSTIISNA CYGSVFSFLC YLIGKLSREF QEERITQADN RESNASSESR FISCFGQLMF
     PCFVSGLVKA DQQILAGFLV TKFMHSNPSL SLINVAEASL RRYLDKQLES LEHLEDSFAE
     SSDFETLKNT VSSLRGTSKE VIRSALASLS NCTNSR