LOCUS       NP_001033691             555 aa            linear   ROD 28-APR-2025
DEFINITION  MARVEL domain-containing protein 2 isoform 1 [Mus musculus].
ACCESSION   NP_001033691
VERSION     NP_001033691.1
DBSOURCE    REFSEQ: accession NM_001038602.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Siegerist,F., Kliewe,F., Hammer,E., Schakau,P., Chi Soh,J.E.,
            Weber,C., Lindenmeyer,M., Reichelt-Wurm,S., Drenic,V.,
            Chatziantoniou,C., Chadjichristos,C.E., Zhang,Y., Simm,S.,
            Banas,M.C., Nauck,M., Volker,U. and Endlich,N.
  TITLE     The role of the tricellular junction protein ILDR2 in
            glomerulopathies: Expression patterns and functional insights
  JOURNAL   iScience 27 (12), 111329 (2024)
   PUBMED   39640577
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Hofling,C., Rossner,S., Flachmeyer,B., Krueger,M., Hartig,W. and
            Michalski,D.
  TITLE     Tricellulin, alpha-Catenin and Microfibrillar-Associated Protein 5
            Exhibit Concomitantly Altered Immunosignals along with Vascular,
            Extracellular and Cytoskeletal Elements after Experimental Focal
            Cerebral Ischemia
  JOURNAL   Int J Mol Sci 24 (15), 11893 (2023)
   PUBMED   37569268
  REMARK    GeneRIF: Tricellulin, alpha-Catenin and Microfibrillar-Associated
            Protein 5 Exhibit Concomitantly Altered Immunosignals along with
            Vascular, Extracellular and Cytoskeletal Elements after
            Experimental Focal Cerebral Ischemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Kim,Y.S., Fan,R., Lith,S.C., Dicke,A.K., Drexler,H.C.A., Kremer,L.,
            Kuempel-Rink,N., Hekking,L., Stehling,M. and Bedzhov,I.
  TITLE     Rap1 controls epiblast morphogenesis in sync with the pluripotency
            states transition
  JOURNAL   Dev Cell 57 (16), 1937-1956 (2022)
   PUBMED   35998584
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Ye,Q., Bhojwani,A. and Hu,J.K.
  TITLE     Understanding the development of oral epithelial organs through
            single cell transcriptomic analysis
  JOURNAL   Development 149 (16) (2022)
   PUBMED   35831953
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Kikuchi,S., Ninomiya,T., Tatsumi,H., Sawada,N. and Kojima,T.
  TITLE     Tricellulin is expressed in autotypic tight junctions of peripheral
            myelinating Schwann cells
  JOURNAL   J Histochem Cytochem 58 (12), 1067-1073 (2010)
   PUBMED   21097846
  REMARK    GeneRIF: The tricellulin may be a component to maintain the
            integrity for PNS myelin function and morphology.
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Raleigh,D.R., Marchiando,A.M., Zhang,Y., Shen,L., Sasaki,H.,
            Wang,Y., Long,M. and Turner,J.R.
  TITLE     Tight junction-associated MARVEL proteins marveld3, tricellulin,
            and occludin have distinct but overlapping functions
  JOURNAL   Mol Biol Cell 21 (7), 1200-1213 (2010)
   PUBMED   20164257
  REMARK    GeneRIF: marvelD3, occludin, and tricellulin define the tight
            junction-associated MARVEL protein family
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Ikenouchi,J., Sasaki,H., Tsukita,S., Furuse,M. and Tsukita,S.
  TITLE     Loss of occludin affects tricellular localization of tricellulin
  JOURNAL   Mol Biol Cell 19 (11), 4687-4693 (2008)
   PUBMED   18768749
  REMARK    GeneRIF: Knockdown of occludin caused mislocalization of
            tricellulin to bTJs, implying that occludin supports tricellular
            localization of tricellulin by excluding tricellulin from
            bicellular tight junctions.
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Riazuddin,S., Ahmed,Z.M., Fanning,A.S., Lagziel,A., Kitajiri,S.,
            Ramzan,K., Khan,S.N., Chattaraj,P., Friedman,P.L., Anderson,J.M.,
            Belyantseva,I.A., Forge,A., Riazuddin,S. and Friedman,T.B.
  TITLE     Tricellulin is a tight-junction protein necessary for hearing
  JOURNAL   Am J Hum Genet 79 (6), 1040-1051 (2006)
   PUBMED   17186462
  REMARK    GeneRIF: In the inner ear, tricellulin is concentrated at the
            tricellular tight-junctions in cochlear and vestibular epithelia,
            including the structurally complex and extensive junctions between
            supporting and hair cells.
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Ikenouchi,J., Furuse,M., Furuse,K., Sasaki,H., Tsukita,S. and
            Tsukita,S.
  TITLE     Tricellulin constitutes a novel barrier at tricellular contacts of
            epithelial cells
  JOURNAL   J Cell Biol 171 (6), 939-945 (2005)
   PUBMED   16365161
  REMARK    GeneRIF: In this study, we identify tricellulin, the first integral
            membrane protein that is concentrated at the vertically oriented TJ
            strands of tricellular contacts.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC165159.2 and AK133741.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK133741.1, SRR17784648.911963.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 53.23 cM"
     Protein         1..555
                     /product="MARVEL domain-containing protein 2 isoform 1"
                     /note="MARVEL domain-containing protein 2; tricellulin"
                     /calculated_mol_wt=63532
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Region          118..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4S9; propagated from
                     UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4S9; propagated from
                     UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Region          182..358
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            252..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4S9; propagated from
                     UniProtKB/Swiss-Prot (Q3UZP0.1)"
     Region          443..545
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     CDS             1..555
                     /gene="Marveld2"
                     /gene_synonym="MARVD2; Mrvldc2; Tric; Trica; Tricb; Tricc"
                     /coded_by="NM_001038602.4:62..1729"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS26732.1"
                     /db_xref="GeneID:218518"
                     /db_xref="MGI:MGI:2446166"
ORIGIN      
        1 msssdarsri rdrgysevpr dtscpdgtir tfqslhssel avsadplppp plplqppfgp
       61 sfyssdteep avapdlkpvr rfvpdswknf frgkkkdpew dnpvsdiryi sdgvecsppa
      121 sparanhhpy kdpsrgsqgt fnsqheadam fahdpyasld rrtqtartys ekveeynlry
      181 aymkswagll rilgvvelll gagvfacvta yihkdnewyn lfgytqpygm gglgslgnty
      241 ggyyysgpkt pfvlvvagla wittiiilvl gmsmyyrtil ldsnwwplte fgvnvalfil
      301 ymaaaivyvn dtnrgglcyy plfntpmnam fcrveggqia amiflfvtmi vylvsalvcl
      361 klwrheaarr hrefleqqei ndpslsskrk mceaaisdrq rdqevnvkdl rtttkmtpel
      421 lsghippghi pkpivmpdyv akypviqtdd drerykavfq dqfseykels aevqailrkf
      481 deldtvmsrl phhsenrqeh erisriheef rkkkndpsfl ekkercdylk nklshikqri
      541 qeydkvmnwd tqgyp
//
