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P39059 (COFA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XV) chain

Cleaved into the following 4 chains:

  1. Restin
    Alternative name(s):
    Endostatin-XV
    Related to endostatin
    Restin-I
  2. Restin-2
    Alternative name(s):
    Restin-II
  3. Restin-3
    Alternative name(s):
    Restin-III
  4. Restin-4
    Alternative name(s):
    Restin-IV
Gene names
Name:COL15A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle. Ref.8

Restin potently inhibits angiogenesis By similarity. Ref.8

Subunit structure

Trimer; disulfide-linked. Ref.7 Ref.9

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed predominantly in internal organs such as adrenal gland, pancreas and kidney.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

O-glycosylated; with core 1 or possibly core 8 glycans. An N-terminal peptide contains chondroitin sulfate. Ref.9 Ref.10

Sequence similarities

Belongs to the multiplexin collagen family.

Contains 4 collagen-like domains.

Contains 1 laminin G-like domain.

Caution

The name restin has also been used for CAP-Gly domain-containing linker protein 1 the product of the CLIP1 gene.

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
Differentiation
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainCollagen
Repeat
Signal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred by curator Ref.2. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

collagen catabolic process

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

signal transduction

Non-traceable author statement PubMed 10891348. Source: UniProtKB

   Cellular_componentcollagen type XV trimer

Traceable author statement Ref.2. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of membrane

Non-traceable author statement PubMed 10891348. Source: UniProtKB

   Molecular_functionextracellular matrix structural constituent

Inferred by curator Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 13881361Collagen alpha-1(XV) chain
PRO_0000005788
Chain1198 – 1386189Restin
PRO_0000005789
Chain1207 – 1386180Restin-2
PRO_0000423014
Chain1213 – 1386174Restin-3
PRO_0000423015
Chain1221 – 1386166Restin-4
PRO_0000423016

Regions

Domain66 – 249184Laminin G-like
Repeat358 – 408511
Repeat409 – 459512
Repeat460 – 509503
Repeat510 – 555464
Domain619 – 68062Collagen-like 1
Domain681 – 73151Collagen-like 2
Domain823 – 86543Collagen-like 3
Domain879 – 92749Collagen-like 4
Region229 – 555327Nonhelical region 1 (NC1)
Region358 – 5551984 X tandem repeats
Region556 – 57318Triple-helical region 1 (COL1)
Region574 – 61845Nonhelical region 2 (NC2)
Region619 – 732114Triple-helical region 2 (COL2)
Region733 – 76331Nonhelical region 3 (NC3)
Region764 – 79835Triple-helical region 3 (COL3)
Region799 – 82224Nonhelical region 4 (NC4)
Region823 – 86745Triple-helical region 4 (COL4)
Region868 – 87811Nonhelical region 5 (NC5)
Region879 – 94971Triple-helical region 5 (COL5)
Region950 – 98334Nonhelical region 6 (NC6)
Region984 – 101330Triple-helical region 6 (COL6)
Region1014 – 102714Nonhelical region 7 (NC7)
Region1028 – 104518Triple-helical region 7 (COL7)
Region1046 – 10527Nonhelical region 8 (NC8)
Region1053 – 110755Triple-helical region 8 (COL8)
Region1108 – 111710Nonhelical region 9 (NC9)
Region1118 – 113215Triple-helical region 9 (COL9)
Region1133 – 1388256Nonhelical region 10 (NC10)

Amino acid modifications

Glycosylation2651O-linked (GalNAc...) Ref.10
Glycosylation3061N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation6871N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential
Glycosylation8141N-linked (GlcNAc...) Potential
Glycosylation10461N-linked (GlcNAc...) Potential
Disulfide bond1237 ↔ 1377 Ref.7 Ref.9
Disulfide bond1339 ↔ 1369 Ref.7 Ref.9

Natural variations

Natural variant1631R → H.
Corresponds to variant rs2075662 [ dbSNP | Ensembl ].
VAR_033787
Natural variant2041M → V. Ref.4
Corresponds to variant rs2075663 [ dbSNP | Ensembl ].
VAR_033788
Natural variant3911T → M.
Corresponds to variant rs10988532 [ dbSNP | Ensembl ].
VAR_033789
Natural variant4421A → T.
Corresponds to variant rs16918128 [ dbSNP | Ensembl ].
VAR_033790
Natural variant4461G → R.
Corresponds to variant rs35934703 [ dbSNP | Ensembl ].
VAR_033791
Natural variant5041G → V.
Corresponds to variant rs2297603 [ dbSNP | Ensembl ].
VAR_048776
Natural variant5061E → D.
Corresponds to variant rs35250850 [ dbSNP | Ensembl ].
VAR_033792
Natural variant5311P → R.
Corresponds to variant rs35529307 [ dbSNP | Ensembl ].
VAR_033793
Natural variant7051P → L.
Corresponds to variant rs41308900 [ dbSNP | Ensembl ].
VAR_061114
Natural variant9891K → R.
Corresponds to variant rs35642150 [ dbSNP | Ensembl ].
VAR_033794
Natural variant10011K → R.
Corresponds to variant rs35544077 [ dbSNP | Ensembl ].
VAR_033795
Natural variant13321V → I.
Corresponds to variant rs10519 [ dbSNP | Ensembl ].
VAR_033796

Experimental info

Sequence conflict101C → S in BAA04762. Ref.4
Sequence conflict491V → D in AAA58429. Ref.1
Sequence conflict94 – 952SV → RA in AAA58429. Ref.1
Sequence conflict94 – 952SV → RA in BAA04762. Ref.4
Sequence conflict1501A → P in AAA58429. Ref.1
Sequence conflict4091A → R in AAA58429. Ref.1
Sequence conflict4091A → R in AAC78500. Ref.2
Sequence conflict11341L → LLGELIPIPADSPPPPALSS N in AAC78500. Ref.2
Sequence conflict1178 – 119720Missing in AAC78500. Ref.2
Sequence conflict12271F → V in AAC78500. Ref.2

Secondary structure

........... 1388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39059 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: AF54DDCC136C3745

FASTA1,388141,720
        10         20         30         40         50         60 
MAPRRNNGQC WCLLMLLSVS TPLPAVTQTR GATETASQGH LDLTQLIGVP LPSSVSFVTG 

        70         80         90        100        110        120 
YGGFPAYSFG PGANVGRPAR TLIPSTFFRD FAISVVVKPS STRGGVLFAI TDAFQKVIYL 

       130        140        150        160        170        180 
GLRLSGVEDG HQRIILYYTE PGSHVSQEAA AFSVPVMTHR WNRFAMIVQG EEVTLLVNCE 

       190        200        210        220        230        240 
EHSRIPFQRS SQALAFESSA GIFMGNAGAT GLERFTGSLQ QLTVHPDPRT PEELCDPEES 

       250        260        270        280        290        300 
SASGETSGLQ EADGVAEILE AVTYTQASPK EAKVEPINTP PTPSSPFEDM ELSGEPVPEG 

       310        320        330        340        350        360 
TLETTNMSII QHSSPKQGSG EILNDTLEGV HSVDGDPITD SGSGAGAFLD IAEEKNLAAT 

       370        380        390        400        410        420 
AAGLAEVPIS TAGEAEASSV PTGGPTLSMS TENPEEGVTP GPDNEERLAA TAAGEAEALA 

       430        440        450        460        470        480 
SMPGEVEASG VAPGELDLSM SAQSLGEEAT VGPSSEDSLT TAAAATEVSL STFEDEEASG 

       490        500        510        520        530        540 
VPTDGLAPLT ATMAPERAVT SGPGDEEDLA AATTEEPLIT AGGEESGSPP PDGPPLPLPT 

       550        560        570        580        590        600 
VAPERWITPA QREHVGMKGQ AGPKGEKGDA GEELPGPPEP SGPVGPTAGA EAEGSGLGWG 

       610        620        630        640        650        660 
SDVGSGSGDL VGSEQLLRGP PGPPGPPGLP GIPGKPGTDV FMGPPGSPGE DGPAGEPGPP 

       670        680        690        700        710        720 
GPEGQPGVDG ATGLPGMKGE KGARGPNGSV GEKGDPGNRG LPGPPGKKGQ AGPPGVMGPP 

       730        740        750        760        770        780 
GPPGPPGPPG PGCTMGLGFE DTEGSGSTQL LNEPKLSRPT AAIGLKGEKG DRGPKGERGM 

       790        800        810        820        830        840 
DGASIVGPPG PRGPPGHIKV LSNSLINITH GFMNFSDIPE LVGPPGPDGL PGLPGFPGPR 

       850        860        870        880        890        900 
GPKGDTGLPG FPGLKGEQGE KGEPGAILTE DIPLERLMGK KGEPGMHGAP GPMGPKGPPG 

       910        920        930        940        950        960 
HKGEFGLPGR PGRPGLNGLK GTKGDPGVIM QGPPGLPGPP GPPGPPGAVI NIKGAIFPIP 

       970        980        990       1000       1010       1020 
VRPHCKMPVD TAHPGSPELI TFHGVKGEKG SWGLPGSKGE KGDQGAQGPP GPPLDLAYLR 

      1030       1040       1050       1060       1070       1080 
HFLNNLKGEN GDKGFKGEKG EKGDINGSFL MSGPPGLPGN PGPAGQKGET VVGPQGPPGA 

      1090       1100       1110       1120       1130       1140 
PGLPGPPGFG RPGDPGPPGP PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSN 

      1150       1160       1170       1180       1190       1200 
MDDMLQKAHL VIEGTFIYLR DSTEFFIRVR DGWKKLQLGE LIPIPADSPP PPALSSNPHQ 

      1210       1220       1230       1240       1250       1260 
LLPPPNPISS ANYEKPALHL AALNMPFSGD IRADFQCFKQ ARAAGLLSTY RAFLSSHLQD 

      1270       1280       1290       1300       1310       1320 
LSTIVRKAER YSLPIVNLKG QVLFNNWDSI FSGHGGQFNM HIPIYSFDGR DIMTDPSWPQ 

      1330       1340       1350       1360       1370       1380 
KVIWHGSSPH GVRLVDNYCE AWRTADTAVT GLASPLSTGK ILDQKAYSCA NRLIVLCIEN 


SFMTDARK 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the alpha 1 chain of human type XV collagen and exon-intron organization in the 3' region of the corresponding gene."
Kivirikko S., Heinamaki P., Rehn M.V., Honkanen N., Myers J.C., Pihlajaniemi T.
J. Biol. Chem. 269:4773-4779(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Umbilical cord.
[2]"Complete exon-intron organization of the human gene for the alpha1 chain of type XV collagen (COL15A1) and comparison with the homologous COL18A1 gene."
Haegg P.M., Muona A., Lietard J., Kivirikko S., Pihlajaniemi T.
J. Biol. Chem. 273:17824-17831(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The human alpha 1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1(XVIII) collagen."
Muragaki Y., Abe N., Ninomiya Y., Olsen B.R., Ooshima A.
J. Biol. Chem. 269:4042-4046(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-569, VARIANT VAL-204.
Tissue: Placenta.
[5]"Identification of a previously unknown human collagen chain, alpha 1(XV), characterized by extensive interruptions in the triple-helical region."
Myers J.C., Kivirikko S., Gordon M.K., Dion A.S., Pihlajaniemi T.
Proc. Natl. Acad. Sci. U.S.A. 89:10144-10148(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 544-1252.
[6]"Chromosomal assignment of a gene encoding a new collagen type (COL15A1) to 9q21 --> q22."
Huebner K., Cannizzaro L.A., Jabs E.W., Kivirikko S., Manzone H., Pihlajaniemi T., Myers J.C.
Genomics 14:220-224(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1145, CHROMOSOMAL LOCATION.
Tissue: Placenta.
[7]"Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin."
John H., Radtke K., Staendker L., Forssmann W.G.
Biochim. Biophys. Acta 1747:161-170(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1198-1210; 1207-1219; 1213-1225 AND 1221-1233, IDENTIFICATION OF RESTIN-RELATED PEPTIDES, DISULFIDE BOND.
[8]"Antiangiogenic activity of restin, NC10 domain of human collagen XV: comparison to endostatin."
Ramchandran R., Dhanabal M., Volk R., Waterman M.J.F., Segal M., Lu H., Knebelmann B., Sukhatme V.P.
Biochem. Biophys. Res. Commun. 255:735-739(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells."
Li D., Clark C.C., Myers J.C.
J. Biol. Chem. 275:22339-22347(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, INTERCHAIN DISULFIDE BONDS.
[10]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-265, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25286 mRNA. Translation: AAA58429.1.
L25280 expand/collapse EMBL AC list , L25281, L25282, L25283, L25284, L25285, AF052956, AF052957, AF052958, AF052959, AF052960, AF052961, AF052962, AF052963, AF052964, AF052965, AF052966, AF052967, AF052968, AF052969, AF052970, AF052971, AF052972, AF052973, AF052974, AF052975 Genomic DNA. Translation: AAC78500.1.
AL136084, AL354923 Genomic DNA. Translation: CAI17044.2.
AL354923, AL136084 Genomic DNA. Translation: CAI12548.2.
D21230 mRNA. Translation: BAA04762.1.
L01697 mRNA. No translation available.
CCDSCCDS35081.1.
PIRA53317.
RefSeqNP_001846.3. NM_001855.4.
UniGeneHs.409034.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N3FX-ray2.00A/B1133-1186[»]
ProteinModelPortalP39059.
SMRP39059. Positions 1133-1186, 1215-1382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107702. 2 interactions.
IntActP39059. 2 interactions.
STRING9606.ENSP00000364140.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP39059.

Polymorphism databases

DMDM68839886.

Proteomic databases

MaxQBP39059.
PaxDbP39059.
PRIDEP39059.

Protocols and materials databases

DNASU1306.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375001; ENSP00000364140; ENSG00000204291.
GeneID1306.
KEGGhsa:1306.
UCSCuc004azb.2. human.

Organism-specific databases

CTD1306.
GeneCardsGC09P101705.
H-InvDBHIX0008227.
HGNCHGNC:2192. COL15A1.
HPAHPA017913.
HPA017915.
MIM120325. gene.
neXtProtNX_P39059.
PharmGKBPA26708.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000231591.
HOVERGENHBG080337.
InParanoidP39059.
KOK08135.
OMAPELITFH.
OrthoDBEOG7NSB2B.
PhylomeDBP39059.
TreeFamTF315821.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeP39059.
CleanExHS_COL15A1.
GenevestigatorP39059.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR008985. ConA-like_lec_gl_sf.
IPR001791. Laminin_G.
[Graphical view]
PfamPF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view]
SMARTSM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.
ProtoNetSearch...

Other

ChiTaRSCOL15A1. human.
GeneWikiCollagen,_type_XV,_alpha_1.
GenomeRNAi1306.
NextBio5345.
PROP39059.
SOURCESearch...

Entry information

Entry nameCOFA1_HUMAN
AccessionPrimary (citable) accession number: P39059
Secondary accession number(s): Q5T6J4, Q9UDC5, Q9Y4W4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM