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TSN36_DANRE
ID   TSN36_DANRE             Reviewed;         243 AA.
AC   Q6NWG0; Q6DGE3;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Tetraspanin-36 {ECO:0000312|ZFIN:ZDB-GENE-040718-248};
DE   AltName: Full=Tetraspanin-3c {ECO:0000303|PubMed:24734316};
GN   Name=tspan36 {ECO:0000312|ZFIN:ZDB-GENE-040718-248};
GN   Synonyms=tspan3c {ECO:0000303|PubMed:24734316};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN   [1] {ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000312|EMBL:AAH76407.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Singapore; TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
RP   MUTAGENESIS OF ILE-18.
RX   PubMed=24734316; DOI=10.1111/pcmr.12192;
RA   Inoue S., Kondo S., Parichy D.M., Watanabe M.;
RT   "Tetraspanin 3c requirement for pigment cell interactions and boundary
RT   formation in zebrafish adult pigment stripes.";
RL   Pigment Cell Melanoma Res. 27:190-200(2014).
CC   -!- FUNCTION: Plays a role in migration and segregation of pigment cells
CC       (melanophores and xanthophores). Contributes to pigment stripe
CC       patterning in the epidermis. {ECO:0000269|PubMed:24734316}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:24734316}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:24734316}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Mainly found in the Golgi apparatus.
CC       {ECO:0000269|PubMed:24734316}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in melanophores and
CC       xanthophores. Also detected in eye, brain, heart, skin, fin, testis and
CC       ovary. {ECO:0000269|PubMed:24734316}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:24734316}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000255,
CC       ECO:0000255|RuleBase:RU361218}.
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DR   EMBL; AL928845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT956087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC067604; AAH67604.2; -; mRNA.
DR   EMBL; BC076407; AAH76407.1; -; mRNA.
DR   RefSeq; NP_001002748.1; NM_001002748.2.
DR   AlphaFoldDB; Q6NWG0; -.
DR   SMR; Q6NWG0; -.
DR   STRING; 7955.ENSDARP00000032359; -.
DR   PaxDb; Q6NWG0; -.
DR   Ensembl; ENSDART00000032498; ENSDARP00000032359; ENSDARG00000024540.
DR   Ensembl; ENSDART00000189986; ENSDARP00000151391; ENSDARG00000109488.
DR   GeneID; 437021; -.
DR   KEGG; dre:437021; -.
DR   CTD; 437021; -.
DR   ZFIN; ZDB-GENE-040718-248; tspan36.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000164634; -.
DR   HOGENOM; CLU_055524_5_2_1; -.
DR   InParanoid; Q6NWG0; -.
DR   OMA; LRESKCG; -.
DR   OrthoDB; 1467737at2759; -.
DR   PhylomeDB; Q6NWG0; -.
DR   TreeFam; TF316345; -.
DR   PRO; PR:Q6NWG0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000024540; Expressed in spleen and 30 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043473; P:pigmentation; IMP:ZFIN.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   PANTHER; PTHR19282; PTHR19282; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   SUPFAM; SSF48652; SSF48652; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Tetraspanin-36"
FT                   /id="PRO_0000442536"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..49
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..208
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         18
FT                   /note="I->R: In dali; retained in the endoplasmic
FT                   reticulum. Incomplete N-glycosylation. Defective migration
FT                   and cell-cell interaction between melanophores and
FT                   xanthophores, leading to abnormal pigment stripe
FT                   patterning."
FT                   /evidence="ECO:0000269|PubMed:24734316"
SQ   SEQUENCE   243 AA;  26885 MW;  F8499A0C77C94ADF CRC64;
     MDCGIITSKT ILLLLSLIFW AAGAALAYVG SYVIKSYNNF EDFMSDRHTL IPAAIIIGVA
     VVMFIIGFVG CCATLRESKV GLGLFLIIIM LIFAAEVTAF VFGIIYRGRI RGDLEKSMND
     VFLKYDGLNS ETHAVDYLQS QLECCGVKNQ TDWTLTSWFA QHNNTVPQSC CKANMTQCTG
     QLSQPDLLNT QGCEAKLEQV LQDVLSYAML VILGFAIIKF FGMLSVCVIT CKSKKNEYQP
     LYA
 
 
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