LOCUS       NM_022122               1876 bp    mRNA    linear   PRI 04-APR-2024
DEFINITION  Homo sapiens matrix metallopeptidase 27 (MMP27), mRNA.
ACCESSION   NM_022122
VERSION     NM_022122.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1876)
  AUTHORS   Park,H.S., Ko,K.H., Kim,J.O., An,H.J., Kim,Y.R., Kim,J.H., Lee,W.S.
            and Kim,N.K.
  TITLE     Association Study between the Polymorphisms of Matrix
            Metalloproteinase (MMP) Genes and Idiopathic Recurrent Pregnancy
            Loss
  JOURNAL   Genes (Basel) 10 (5), 347 (2019)
   PUBMED   31067818
  REMARK    GeneRIF: Two polymorphisms of MMP-8 and MMP-27 were significantly
            associated with recurrent pregnancy loss (RPL) risk, both
            individually and in combination. Therefore, these two polymorphisms
            are potential biomarkers for RPL susceptibility.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 1876)
  AUTHORS   Cominelli,A., Gaide Chevronnay,H.P., Lemoine,P., Courtoy,P.J.,
            Marbaix,E. and Henriet,P.
  TITLE     Matrix metalloproteinase-27 is expressed in CD163+/CD206+ M2
            macrophages in the cycling human endometrium and in superficial
            endometriotic lesions
  JOURNAL   Mol Hum Reprod 20 (8), 767-775 (2014)
   PUBMED   24810263
  REMARK    GeneRIF: MMP-27 is expressed in a subset of endometrial macrophages
            related to menstruation and in ovarian and peritoneal endometriotic
            lesions.
REFERENCE   3  (bases 1 to 1876)
  AUTHORS   Cominelli,A., Halbout,M., N'Kuli,F., Lemoine,P., Courtoy,P.J.,
            Marbaix,E., Tyteca,D. and Henriet,P.
  TITLE     A unique C-terminal domain allows retention of matrix
            metalloproteinase-27 in the endoplasmic reticulum
  JOURNAL   Traffic 15 (4), 401-417 (2014)
   PUBMED   24548619
  REMARK    GeneRIF: MMP-27 is efficiently retained within the ER due to its
            unique CTE, which does not lead to stable membrane insertion. This
            could represent a novel ER retention system
REFERENCE   4  (bases 1 to 1876)
  AUTHORS   Eeles,R.A., Olama,A.A., Benlloch,S., Saunders,E.J.,
            Leongamornlert,D.A., Tymrakiewicz,M., Ghoussaini,M., Luccarini,C.,
            Dennis,J., Jugurnauth-Little,S., Dadaev,T., Neal,D.E., Hamdy,F.C.,
            Donovan,J.L., Muir,K., Giles,G.G., Severi,G., Wiklund,F.,
            Gronberg,H., Haiman,C.A., Schumacher,F., Henderson,B.E., Le
            Marchand,L., Lindstrom,S., Kraft,P., Hunter,D.J., Gapstur,S.,
            Chanock,S.J., Berndt,S.I., Albanes,D., Andriole,G., Schleutker,J.,
            Weischer,M., Canzian,F., Riboli,E., Key,T.J., Travis,R.C.,
            Campa,D., Ingles,S.A., John,E.M., Hayes,R.B., Pharoah,P.D.,
            Pashayan,N., Khaw,K.T., Stanford,J.L., Ostrander,E.A.,
            Signorello,L.B., Thibodeau,S.N., Schaid,D., Maier,C., Vogel,W.,
            Kibel,A.S., Cybulski,C., Lubinski,J., Cannon-Albright,L.,
            Brenner,H., Park,J.Y., Kaneva,R., Batra,J., Spurdle,A.B.,
            Clements,J.A., Teixeira,M.R., Dicks,E., Lee,A., Dunning,A.M.,
            Baynes,C., Conroy,D., Maranian,M.J., Ahmed,S., Govindasami,K.,
            Guy,M., Wilkinson,R.A., Sawyer,E.J., Morgan,A., Dearnaley,D.P.,
            Horwich,A., Huddart,R.A., Khoo,V.S., Parker,C.C., Van As,N.J.,
            Woodhouse,C.J., Thompson,A., Dudderidge,T., Ogden,C., Cooper,C.S.,
            Lophatananon,A., Cox,A., Southey,M.C., Hopper,J.L., English,D.R.,
            Aly,M., Adolfsson,J., Xu,J., Zheng,S.L., Yeager,M., Kaaks,R.,
            Diver,W.R., Gaudet,M.M., Stern,M.C., Corral,R., Joshi,A.D.,
            Shahabi,A., Wahlfors,T., Tammela,T.L., Auvinen,A., Virtamo,J.,
            Klarskov,P., Nordestgaard,B.G., Roder,M.A., Nielsen,S.F.,
            Bojesen,S.E., Siddiq,A., Fitzgerald,L.M., Kolb,S., Kwon,E.M.,
            Karyadi,D.M., Blot,W.J., Zheng,W., Cai,Q., McDonnell,S.K.,
            Rinckleb,A.E., Drake,B., Colditz,G., Wokolorczyk,D.,
            Stephenson,R.A., Teerlink,C., Muller,H., Rothenbacher,D.,
            Sellers,T.A., Lin,H.Y., Slavov,C., Mitev,V., Lose,F.,
            Srinivasan,S., Maia,S., Paulo,P., Lange,E., Cooney,K.A.,
            Antoniou,A.C., Vincent,D., Bacot,F., Tessier,D.C., Kote-Jarai,Z.
            and Easton,D.F.
  CONSRTM   COGS-Cancer Research UK GWAS-ELLIPSE (part of GAME-ON) Initiative;
            Australian Prostate Cancer Bioresource; UK Genetic Prostate Cancer
            Study Collaborators/British Association of Urological Surgeons'
            Section of Oncology; UK ProtecT (Prostate testing for cancer and
            Treatment) Study Collaborators; PRACTICAL (Prostate Cancer
            Association Group to Investigate Cancer-Associated Alterations in
            the Genome) Consortium
  TITLE     Identification of 23 new prostate cancer susceptibility loci using
            the iCOGS custom genotyping array
  JOURNAL   Nat Genet 45 (4), 385-391 (2013)
   PUBMED   23535732
REFERENCE   5  (bases 1 to 1876)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (bases 1 to 1876)
  AUTHORS   Wojciechowski,R., Bailey-Wilson,J.E. and Stambolian,D.
  TITLE     Association of matrix metalloproteinase gene polymorphisms with
            refractive error in Amish and Ashkenazi families
  JOURNAL   Invest Ophthalmol Vis Sci 51 (10), 4989-4995 (2010)
   PUBMED   20484597
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (bases 1 to 1876)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (bases 1 to 1876)
  AUTHORS   Nagase,H. and Woessner,J.F. Jr.
  TITLE     Matrix metalloproteinases
  JOURNAL   J Biol Chem 274 (31), 21491-21494 (1999)
   PUBMED   10419448
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000647.5, AY358752.1,
            BX102293.1 and AP000851.4.
            
            On May 17, 2019 this sequence version replaced NM_022122.2.
            
            Summary: Proteins of the matrix metalloproteinase (MMP) family are
            involved in the breakdown of extracellular matrix in normal
            physiological processes, such as embryonic development,
            reproduction, and tissue remodeling, as well as in disease
            processes, such as arthritis and metastasis. Most MMP's are
            secreted as inactive proproteins which are activated when cleaved
            by extracellular proteinases. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358752.1, AF195192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596, SAMEA2162823
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260229.5/ ENSP00000260229.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-32                AP000647.5         6488-6519           c
            33-851              AY358752.1         1-819
            852-1515            BX102293.1         68-731
            1516-1679           AY358752.1         1484-1647
            1680-1876           AP000851.4         144587-144783       c
FEATURES             Location/Qualifiers
     source          1..1876
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.2"
     gene            1..1876
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /note="matrix metallopeptidase 27"
                     /db_xref="GeneID:64066"
                     /db_xref="HGNC:HGNC:14250"
                     /db_xref="MIM:618101"
     exon            1..157
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     CDS             56..1597
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /note="matrix metalloprotease 27; matrix
                     metalloproteinase-27"
                     /codon_start=1
                     /product="matrix metalloproteinase-27 precursor"
                     /protein_id="NP_071405.2"
                     /db_xref="CCDS:CCDS8319.1"
                     /db_xref="GeneID:64066"
                     /db_xref="HGNC:HGNC:14250"
                     /db_xref="MIM:618101"
                     /translation="MKRLLLLFLFFITFSSAFPLVRMTENEENMQLAQAYLNQFYSLE
                     IEGNHLVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIMKTPRCGVPDVGQYGYT
                     LPGWRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAF
                     RTRVHGRCPRYFDGPLGVLGHAFPPGPGLGGDTHFDEDENWTKDGAGFNLFLVAAHEF
                     GHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYGGLPKEPAKPKEPTIP
                     HACDPDLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYE
                     NPRDKILVFKDENFWMIRGYAVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFV
                     GIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQYKGFFFFSRGSKQFEYDIKT
                     KNITRIMRTNTWFQCKEPKNSSFGFDINKEKAHSGGIKILYHKSLSLFIFGIVHLLKN
                     TSIYQ"
     exon            158..396
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            397..545
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            546..674
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            675..836
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            837..957
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            958..1088
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            1089..1248
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            1249..1352
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     exon            1353..1876
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1853..1858
                     /regulatory_class="polyA_signal_sequence"
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /note="hexamer: ATTAAA"
     polyA_site      1876
                     /gene="MMP27"
                     /gene_synonym="MMP-27"
                     /note="major polyA site"
ORIGIN      
        1 attattttct aaattctgtg ctaacagaac cggcttcagc tgaagaaaga gaggaatgaa
       61 gcgccttctg cttctgtttt tgttctttat aacattttct tctgcatttc ccttagtccg
      121 gatgacggaa aatgaagaaa atatgcaact ggctcaggca tatctcaacc agttctactc
      181 tcttgaaata gaagggaatc atcttgttca aagcaagaat aggagtctca tagatgacaa
      241 aattcgggaa atgcaagcat tttttggatt gacagtgact ggaaaactgg actcaaacac
      301 ccttgagatc atgaagacac ccaggtgtgg ggtgcctgat gtgggccagt atggctacac
      361 cctccctggg tggagaaaat acaacctcac ctacagaata ataaactata ctccggatat
      421 ggcacgagct gctgtggatg aggctatcca agaaggttta gaagtgtgga gcaaagtcac
      481 tccactaaaa ttcaccaaga tttcaaaggg gattgcagac atcatgattg cctttaggac
      541 tcgagtccat ggtcggtgtc ctcgctattt tgatggtccc ttgggagtgc ttggccatgc
      601 ctttcctcct ggtccgggtc tgggtggtga cactcatttt gatgaggatg aaaactggac
      661 caaggatgga gcaggattca acttgtttct tgtggctgct catgaatttg gtcatgcact
      721 ggggctctct cactccaatg atcaaacagc cttgatgttc ccaaattatg tctccctgga
      781 tcccagaaaa tacccacttt ctcaggatga tatcaatgga atccagtcca tctatggagg
      841 tctgcctaag gaacctgcta agccaaagga acccactata ccccatgcct gtgaccctga
      901 cttgactttt gacgctatca caactttccg cagagaagta atgttcttta aaggcaggca
      961 cctatggagg atctattatg atatcacgga tgttgagttt gaattaattg cttcattctg
     1021 gccatctctg ccagctgatc tgcaagctgc atacgagaac cccagagata agattctggt
     1081 ttttaaagat gaaaacttct ggatgatcag aggatatgct gtcttgccag attatcccaa
     1141 atccatccat acattaggtt ttccaggacg tgtgaagaaa atagatgcag ccgtctgtga
     1201 taagaccaca agaaaaacct acttctttgt gggcatttgg tgctggaggt ttgatgaaat
     1261 gacccaaacc atggacaaag ggttcccgca gagagtggta aaacactttc ctggaatcag
     1321 tatccgtgtt gatgctgctt tccagtacaa aggattcttc tttttcagcc gtggatcaaa
     1381 gcaatttgaa tacgacatta agacaaagaa tattacccga atcatgagaa ctaatacttg
     1441 gtttcaatgc aaagaaccaa agaactcctc atttggtttt gatatcaaca aggaaaaagc
     1501 acattcagga ggcataaaga tattgtatca taagagttta agcttgttta tttttggtat
     1561 tgttcatttg ctgaaaaaca cttctattta tcaataaatt catagaccta aaataaacct
     1621 caacaggtct tttaatataa attctgcttc aaaatagaat aaaaccattc tttaacaaca
     1681 agttgctggt cctagttcta aatatccaaa ttcaatggcc attttgagct gcctgattct
     1741 tttaatagga agttattatg tagaaacaaa aatctctgac tgtactttaa gcctatttca
     1801 tgctttgtgg acttggagaa gacatgtctt ataactgaat actgaaacat ttattaaacc
     1861 aatctttagc attcta
//
