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TMM8B_HUMAN
ID   TMM8B_HUMAN             Reviewed;         472 AA.
AC   A6NDV4; B3KQF3; O75539; Q49AB1; Q4KMX5; Q5TCW5; Q9HBY2; Q9P0U7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Transmembrane protein 8B;
DE   AltName: Full=Nasopharyngeal carcinoma-associated gene 6 protein;
DE   AltName: Full=Protein NAG-5;
DE   AltName: Full=Protein NGX6;
GN   Name=TMEM8B; Synonyms=C9orf127, NGX6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=11565907; DOI=10.1023/a:1010912311564;
RA   Li J., Tan C., Xiang Q., Zhang X., Ma J., Wang J.-R., Yang J., Li W.-F.,
RA   Shen S.-R., Liang S., Li G.-Y.;
RT   "Proteomic detection of changes in protein synthesis induced by NGX6
RT   transfected in human nasopharyngeal carcinoma cells.";
RL   J. Protein Chem. 20:265-271(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
RP   INDUCTION.
RX   PubMed=15498789; DOI=10.1093/carcin/bgh312;
RA   Ma J., Zhou J., Fan S., Wang L.-L., Li X.-L., Yan Q., Zhou M., Liu H.-Y.,
RA   Zhang Q., Zhou H., Gan K., Li Z., Peng C., Xiong W., Tan C., Shen S.-R.,
RA   Yang J., Li J., Li G.-Y.;
RT   "Role of a novel EGF-like domain-containing gene NGX6 in cell adhesion
RT   modulation in nasopharyngeal carcinoma cells.";
RL   Carcinogenesis 26:281-291(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=15723283; DOI=10.1002/jcb.20393;
RA   Wang L.-L., Ma J., Li J., Li X.-L., Zhang Q., Peng S.-P., Peng C., Zhou M.,
RA   Xiong W., Yang J., Zhou J., Fan S., Tan C., Yan Q., Shen S.-R., Li G.-Y.;
RT   "NGX6 gene inhibits cell proliferation and plays a negative role in EGFR
RT   pathway in nasopharyngeal carcinoma cells.";
RL   J. Cell. Biochem. 95:64-73(2005).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17641538; DOI=10.1159/000106073;
RA   Peng S.P., Li X.-L., Wang L., Ou-Yang J., Ma J., Wang L.-L., Liu H.-Y.,
RA   Zhou M., Tang Y.-L., Li W.-S., Luo X.-M., Cao L., Tang K., Shen S.-R.,
RA   Li G.-Y.;
RT   "The role of NGX6 and its deletion mutants in the proliferation, adhesion
RT   and migration of nasopharyngeal carcinoma 5-8F cells.";
RL   Oncology 71:273-281(2006).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH EZR.
RX   PubMed=17270023; DOI=10.1111/j.1349-7006.2007.00410.x;
RA   Peng S.-P., Fan S., Li X.-L., Wang L., Liu H.-Y., Zhou M., Wang L.-L.,
RA   Shen S.-R., Li G.-Y.;
RT   "The expression of ezrin in NPC and its interaction with NGX6, a novel
RT   candidate suppressor.";
RL   Cancer Sci. 98:341-349(2007).
CC   -!- FUNCTION: May function as a regulator of the EGFR pathway. Probable
CC       tumor suppressor which may function in cell growth, proliferation and
CC       adhesion. {ECO:0000269|PubMed:15498789, ECO:0000269|PubMed:15723283,
CC       ECO:0000269|PubMed:17270023, ECO:0000269|PubMed:17641538}.
CC   -!- SUBUNIT: Isoform 2 (via its cytoplasmic part) interacts with EZR.
CC       {ECO:0000269|PubMed:15498789, ECO:0000269|PubMed:17270023}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC       {ECO:0000269|PubMed:17641538}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17641538}. Cytoplasm {ECO:0000269|PubMed:17641538}.
CC       Nucleus {ECO:0000269|PubMed:17641538}. Mitochondrion
CC       {ECO:0000269|PubMed:17641538}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:17641538}. Note=Also detected in mitochondrion and
CC       endoplasmic reticulum (PubMed:17641538).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A6NDV4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6NDV4-2; Sequence=VSP_033452, VSP_033453;
CC       Name=3;
CC         IsoId=A6NDV4-3; Sequence=VSP_033450, VSP_033451, VSP_033452,
CC                                  VSP_033453;
CC   -!- INDUCTION: Isoform 2 is down-regulated in nasopharyngeal carcinoma
CC       cells. {ECO:0000269|PubMed:15498789}.
CC   -!- PTM: Isoform 2 is N-glycosylated. {ECO:0000269|PubMed:15498789}.
CC   -!- SIMILARITY: Belongs to the TMEM8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC28644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAF34820.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAF34820.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; AF149297; AAF34820.1; ALT_SEQ; mRNA.
DR   EMBL; AF188239; AAG29055.1; -; mRNA.
DR   EMBL; AF070572; AAC28644.1; ALT_INIT; mRNA.
DR   EMBL; AK074844; BAG52015.1; -; mRNA.
DR   EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58325.1; -; Genomic_DNA.
DR   EMBL; BC041377; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC098265; AAH98265.1; -; mRNA.
DR   EMBL; BC098296; AAH98296.1; -; mRNA.
DR   EMBL; BC099733; AAH99733.1; -; mRNA.
DR   CCDS; CCDS43800.1; -. [A6NDV4-1]
DR   CCDS; CCDS6595.1; -. [A6NDV4-2]
DR   RefSeq; NP_001036054.1; NM_001042589.2. [A6NDV4-1]
DR   RefSeq; NP_001036055.1; NM_001042590.2.
DR   RefSeq; NP_057530.2; NM_016446.3. [A6NDV4-2]
DR   AlphaFoldDB; A6NDV4; -.
DR   BioGRID; 119714; 11.
DR   IntAct; A6NDV4; 1.
DR   MINT; A6NDV4; -.
DR   STRING; 9606.ENSP00000367227; -.
DR   TCDB; 1.N.2.1.7; the myoblast fusion complex (mfc) family.
DR   GlyGen; A6NDV4; 2 sites.
DR   iPTMnet; A6NDV4; -.
DR   PhosphoSitePlus; A6NDV4; -.
DR   BioMuta; TMEM8B; -.
DR   jPOST; A6NDV4; -.
DR   MassIVE; A6NDV4; -.
DR   PaxDb; A6NDV4; -.
DR   PeptideAtlas; A6NDV4; -.
DR   PRIDE; A6NDV4; -.
DR   ProteomicsDB; 931; -. [A6NDV4-1]
DR   ProteomicsDB; 932; -. [A6NDV4-2]
DR   ProteomicsDB; 933; -. [A6NDV4-3]
DR   TopDownProteomics; A6NDV4-2; -. [A6NDV4-2]
DR   Antibodypedia; 26101; 155 antibodies from 20 providers.
DR   DNASU; 51754; -.
DR   Ensembl; ENST00000377988.6; ENSP00000367227.2; ENSG00000137103.20. [A6NDV4-1]
DR   Ensembl; ENST00000377991.9; ENSP00000367230.4; ENSG00000137103.20. [A6NDV4-1]
DR   Ensembl; ENST00000377996.5; ENSP00000367235.1; ENSG00000137103.20. [A6NDV4-2]
DR   Ensembl; ENST00000439587.6; ENSP00000395810.2; ENSG00000137103.20. [A6NDV4-2]
DR   Ensembl; ENST00000650015.1; ENSP00000497766.1; ENSG00000137103.20. [A6NDV4-1]
DR   GeneID; 51754; -.
DR   KEGG; hsa:51754; -.
DR   UCSC; uc003zyk.4; human. [A6NDV4-1]
DR   CTD; 51754; -.
DR   DisGeNET; 51754; -.
DR   GeneCards; TMEM8B; -.
DR   HGNC; HGNC:21427; TMEM8B.
DR   HPA; ENSG00000137103; Low tissue specificity.
DR   neXtProt; NX_A6NDV4; -.
DR   OpenTargets; ENSG00000137103; -.
DR   PharmGKB; PA165586305; -.
DR   VEuPathDB; HostDB:ENSG00000137103; -.
DR   eggNOG; ENOG502QQ7Q; Eukaryota.
DR   GeneTree; ENSGT00940000157861; -.
DR   HOGENOM; CLU_823768_0_0_1; -.
DR   InParanoid; A6NDV4; -.
DR   OMA; LDCREWN; -.
DR   OrthoDB; 704708at2759; -.
DR   PhylomeDB; A6NDV4; -.
DR   TreeFam; TF331003; -.
DR   PathwayCommons; A6NDV4; -.
DR   SignaLink; A6NDV4; -.
DR   BioGRID-ORCS; 51754; 11 hits in 1085 CRISPR screens.
DR   ChiTaRS; TMEM8B; human.
DR   GeneWiki; C9orf127; -.
DR   GenomeRNAi; 51754; -.
DR   Pharos; A6NDV4; Tbio.
DR   PRO; PR:A6NDV4; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; A6NDV4; protein.
DR   Bgee; ENSG00000137103; Expressed in left ovary and 144 other tissues.
DR   ExpressionAtlas; A6NDV4; baseline and differential.
DR   Genevisible; A6NDV4; HS.
DR   GO; GO:0009986; C:cell surface; IDA:HGNC-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:HGNC-UCL.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; TAS:HGNC-UCL.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR021910; NGX6/PGAP6/MYMK.
DR   PANTHER; PTHR14319; PTHR14319; 1.
DR   Pfam; PF12036; DUF3522; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Cytoplasm;
KW   Disulfide bond; EGF-like domain; Endoplasmic reticulum; Glycoprotein;
KW   Growth regulation; Membrane; Mitochondrion; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..472
FT                   /note="Transmembrane protein 8B"
FT                   /id="PRO_0000333039"
FT   TOPO_DOM        1..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..292
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..315
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..342
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..405
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          182..221
FT                   /note="EGF-like"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        186..196
FT                   /evidence="ECO:0000250"
FT   DISULFID        190..209
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..220
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..81
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033450"
FT   VAR_SEQ         82..93
FT                   /note="GGVLSLELQLNA -> MWRPHFHTCPPQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033451"
FT   VAR_SEQ         274..337
FT                   /note="FYHACDQPGIVVFCIMDYDVLQFCDFLGSLMSVWVTVIAMARLQPVVKQVLY
FT                   LLGAMLLSMALQ -> VCGGVCILSLGACAWWWVTVCISTTFSEGLGMSVPSLCLLQTE
FT                   TAVLPKLSCIDNGHFCKTHWSK (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11565907,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_033452"
FT   VAR_SEQ         338..472
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11565907,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_033453"
FT   CONFLICT        178
FT                   /note="R -> W (in Ref. 6; AAH98296)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  51941 MW;  3E5EA4495CF54389 CRC64;
     MNMPQSLGNQ PLPPEPPSLG TPAEGPGTTS PPEHCWPVRP TLRNELDTFS VHFYIFFGPS
     VALPPERPAV FAMRLLPVLD SGGVLSLELQ LNASSVRQEN VTVFGCLTHE VPLSLGDAAV
     TCSKESLAGF LLSVSATTRV ARLRIPFPQT GTWFLALRSL CGVGPRFVRC RNATAEVRMR
     TFLSPCVDDC GPYGQCKLLR THNYLYAACE CKAGWRGWGC TDSADALTYG FQLLSTLLLC
     LSNLMFLPPV VLAIRSRYVL EAAVYTFTMF FSTFYHACDQ PGIVVFCIMD YDVLQFCDFL
     GSLMSVWVTV IAMARLQPVV KQVLYLLGAM LLSMALQLDR HGLWNLLGPS LFALGILATA
     WTVRSVRRRH CYPPTWRRWL FYLCPGSLIA GSAVLLYAFV ETRDNYFYIH SIWHMLIAGS
     VGFLLPPRAK TDHGVPSGAR ARGCGYQLCI NEQEELGLVG PGGATVSSIC AS
 
 
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