(data stored in ACNUC31108 zone)

SWISSPROT: TSN1_HUMAN

ID   TSN1_HUMAN              Reviewed;         241 AA.
AC   O60635; D3DQ14; O60745; Q5VST0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAY-2019, entry version 145.
DE   RecName: Full=Tetraspanin-1;
DE            Short=Tspan-1;
DE   AltName: Full=Tetraspan NET-1;
DE   AltName: Full=Tetraspanin TM4-C;
GN   Name=TSPAN1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9714763; DOI=10.1016/S0167-4781(98)00087-6;
RA   Todd S.C., Doctor V.S., Levy S.;
RT   "Sequences and expression of six new members of the tetraspanin/TM4SF
RT   family.";
RL   Biochim. Biophys. Acta 1399:101-104(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Rubinstein E., Serru V., Boucheix C.;
RT   "New tetraspans identified in the EST database.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Puls K.L., Ni J., Liu D., Morahan G., Wright M.D.;
RT   "The molecular characterization of four tetraspanins.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-141; ASN-154; ASN-178 AND
RP   ASN-184, AND MUTAGENESIS OF ASN-141; ASN-154; ASN-178 AND ASN-184.
RX   PubMed=19508227; DOI=10.2174/092986609789071234;
RA   Scholz C.-J., Sauer G., Deissler H.;
RT   "Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes
RT   its transition through the endoplasmic reticulum.";
RL   Protein Pept. Lett. 16:1244-1248(2009).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane
CC       {ECO:0000269|PubMed:19508227}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19508227}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/TSPAN1ID44178ch1p34.html";
DR   EMBL; AF054838; AAC69714.1; -; mRNA.
DR   EMBL; AF065388; AAC17119.1; -; mRNA.
DR   EMBL; AF133425; AAF08364.1; -; mRNA.
DR   EMBL; AK313774; BAG36512.1; -; mRNA.
DR   EMBL; AL672043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06938.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06939.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06940.1; -; Genomic_DNA.
DR   EMBL; BC007290; AAH07290.1; -; mRNA.
DR   EMBL; BC013404; AAH13404.1; -; mRNA.
DR   CCDS; CCDS530.1; -.
DR   PIR; A59262; A59262.
DR   RefSeq; NP_005718.2; NM_005727.3.
DR   BioGrid; 115410; 17.
DR   IntAct; O60635; 4.
DR   STRING; 9606.ENSP00000361072; -.
DR   GlyConnect; 1797; -.
DR   iPTMnet; O60635; -.
DR   PhosphoSitePlus; O60635; -.
DR   BioMuta; TSPAN1; -.
DR   EPD; O60635; -.
DR   jPOST; O60635; -.
DR   MaxQB; O60635; -.
DR   PaxDb; O60635; -.
DR   PeptideAtlas; O60635; -.
DR   PRIDE; O60635; -.
DR   ProteomicsDB; 49488; -.
DR   DNASU; 10103; -.
DR   Ensembl; ENST00000372003; ENSP00000361072; ENSG00000117472.
DR   GeneID; 10103; -.
DR   KEGG; hsa:10103; -.
DR   UCSC; uc001cpd.4; human.
DR   CTD; 10103; -.
DR   DisGeNET; 10103; -.
DR   GeneCards; TSPAN1; -.
DR   HGNC; HGNC:20657; TSPAN1.
DR   HPA; HPA011909; -.
DR   MIM; 613170; gene.
DR   neXtProt; NX_O60635; -.
DR   OpenTargets; ENSG00000117472; -.
DR   PharmGKB; PA134938100; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   eggNOG; ENOG4111IRY; LUCA.
DR   GeneTree; ENSGT00940000158851; -.
DR   HOGENOM; HOG000230651; -.
DR   InParanoid; O60635; -.
DR   KO; K17348; -.
DR   OMA; QGCFKQL; -.
DR   PhylomeDB; O60635; -.
DR   TreeFam; TF352892; -.
DR   GenomeRNAi; 10103; -.
DR   PRO; PR:O60635; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000117472; Expressed in 135 organ(s), highest expression level in bronchial epithelial cell.
DR   Genevisible; O60635; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR000301; Tetraspanin.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   PRINTS; PR00259; TMFOUR.
DR   SUPFAM; SSF48652; SSF48652; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O60635.
DR   SWISS-2DPAGE; O60635.
KW   Complete proteome; Glycoprotein; Lysosome; Membrane; Polymorphism;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    241       Tetraspanin-1.
FT                                /FTId=PRO_0000219234.
FT   TOPO_DOM      1     11       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     12     32       Helical. {ECO:0000255}.
FT   TOPO_DOM     33     52       Extracellular. {ECO:0000255}.
FT   TRANSMEM     53     73       Helical. {ECO:0000255}.
FT   TOPO_DOM     74     88       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     89    109       Helical. {ECO:0000255}.
FT   TOPO_DOM    110    211       Extracellular. {ECO:0000255}.
FT   TRANSMEM    212    232       Helical. {ECO:0000255}.
FT   TOPO_DOM    233    241       Cytoplasmic. {ECO:0000255}.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19508227}.
FT   CARBOHYD    154    154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19508227}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19508227}.
FT   CARBOHYD    184    184       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19508227}.
FT   VARIANT      38     38       S -> F (in dbSNP:rs2234267).
FT                                /FTId=VAR_052327.
FT   VARIANT      87     87       V -> M (in dbSNP:rs2234268).
FT                                /FTId=VAR_034573.
FT   MUTAGEN     141    141       N->A: Loss of glycosylation.
FT                                {ECO:0000269|PubMed:19508227}.
FT   MUTAGEN     154    154       N->A: Loss of glycosylation.
FT                                {ECO:0000269|PubMed:19508227}.
FT   MUTAGEN     178    178       N->A: Loss of glycosylation.
FT                                {ECO:0000269|PubMed:19508227}.
FT   MUTAGEN     184    184       N->A: Loss of glycosylation.
FT                                {ECO:0000269|PubMed:19508227}.
FT   CONFLICT    189    189       K -> E (in Ref. 1; AAC69714).
FT                                {ECO:0000305}.
SQ   SEQUENCE   241 AA;  26301 MW;  AF938AD7147CB884 CRC64;
     MQCFSFIKTM MILFNLLIFL CGAALLAVGI WVSIDGASFL KIFGPLSSSA MQFVNVGYFL
     IAAGVVVFAL GFLGCYGAKT ESKCALVTFF FILLLIFIAE VAAAVVALVY TTMAEHFLTL
     LVVPAIKKDY GSQEDFTQVW NTTMKGLKCC GFTNYTDFED SPYFKENSAF PPFCCNDNVT
     NTANETCTKQ KAHDQKVEGC FNQLLYDIRT NAVTVGGVAA GIGGLELAAM IVSMYLYCNL
     Q
//

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