ID   MALD2_XENTR             Reviewed;         568 AA.
AC   Q0IHQ3; Q28D82;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=MARVEL domain-containing protein 2;
GN   Name=marveld2; Synonyms=mrvldc2; ORFNames=TGas093b21.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Skin;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in the formation of the epithelial barrier.
CC       {ECO:0000250|UniProtKB:Q3UZP0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3UZP0};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3UZP0}. Cell
CC       junction, tight junction {ECO:0000250|UniProtKB:Q3UZP0}. Note=Found at
CC       tricellular contacts. {ECO:0000250|UniProtKB:Q3UZP0}.
CC   -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01324}.
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DR   EMBL; CR855651; CAJ83822.1; -; mRNA.
DR   EMBL; BC123026; AAI23027.1; -; mRNA.
DR   RefSeq; NP_001017292.1; NM_001017292.2.
DR   AlphaFoldDB; Q0IHQ3; -.
DR   SMR; Q0IHQ3; -.
DR   PaxDb; Q0IHQ3; -.
DR   DNASU; 550046; -.
DR   GeneID; 550046; -.
DR   KEGG; xtr:550046; -.
DR   CTD; 153562; -.
DR   Xenbase; XB-GENE-5839559; marveld2.
DR   eggNOG; KOG4796; Eukaryota.
DR   InParanoid; Q0IHQ3; -.
DR   OrthoDB; 335949at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR   GO; GO:0061689; C:tricellular tight junction; IEA:InterPro.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:InterPro.
DR   InterPro; IPR031176; ELL/occludin.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR031177; MARVELD2.
DR   InterPro; IPR010844; Occludin_ELL.
DR   PANTHER; PTHR23288; PTHR23288; 1.
DR   PANTHER; PTHR23288:SF3; PTHR23288:SF3; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   Pfam; PF07303; Occludin_ELL; 1.
DR   PROSITE; PS51225; MARVEL; 1.
DR   PROSITE; PS51980; OCEL; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Coiled coil; Membrane; Reference proteome;
KW   Tight junction; Transmembrane; Transmembrane helix.
FT   CHAIN           1..568
FT                   /note="MARVEL domain-containing protein 2"
FT                   /id="PRO_0000271528"
FT   TOPO_DOM        1..211
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..303
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..568
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          205..379
FT                   /note="MARVEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT   DOMAIN          451..562
FT                   /note="OCEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          462..559
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        136
FT                   /note="G -> E (in Ref. 1; CAJ83822)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   568 AA;  64880 MW;  545EECDD8618F40B CRC64;
     MSGGGSSSGP RSKDRNLNGR SAQYDEVPAD PRHPETNLET LHDRDLALSA DPLPPPPLPL
     HPPFGAEFYP SDSEEPVTTL ELRPVRRFIP DSWKNIFKGK KENPWENPMT EINYTSGGVP
     CSPPRSPSLP ASEPHGKNLA GDSKTVASSY RDPYGGSGGS YNSRREEEAM LPHDPYGSLG
     RQTQTVKTYS ERVEEYNMRY AYMKSWAGLL RILCIVELLL GAAVFACVTA YIHKDNEWYN
     MFGYSQPYGY TASMQGGYYY SGPKTPFVLV VAGLAWIVTI ILLVLGMSMY YRTILLDSTW
     WPLTEFGINI SLFILYMAGA IVYVNDTNRG GLCYYQLFNT PVNASFCRVE GGQTAAIIFL
     FVSMLMYFIS AMVSLKLWRH ESARKRREFL GQEMNPNQIS PPKVMREVAL GNGHMIDVPD
     QQRDMRKVEM KPELLSGYIP AGHIPKPIVM PDYVAKYQAI KAEDERERYK AVFNDQFAEY
     KELHAEVQAV MKKFSELDAV MQKLPRNPEN QHEYERIAKV LQEYQKKKNE PTFLEKKERC
     EYLKNKLSHI KQRIQEYDKV MDWNDGYN