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TCP11_HUMAN
ID   TCP11_HUMAN             Reviewed;         503 AA.
AC   Q8WWU5; B2RCE9; B3KQ27; B7Z7B5; B7Z7G1; B7Z7H4; B7Z7S8; E7EP29; J3KNG1;
AC   Q8NF85; Q9NQZ9; Q9NR39;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=T-complex protein 11 homolog;
GN   Name=TCP11;
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), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11756566; DOI=10.1093/molehr/8.1.24;
RA   Ma Y., Zhang S., Xia Q., Zhang G., Huang X., Huang M., Xiao C., Pan A.,
RA   Sun Y., Lebo R., Milunsky A.;
RT   "Molecular characterization of the TCP11 gene which is the human homologue
RT   of the mouse gene encoding the receptor of fertilization promoting
RT   peptide.";
RL   Mol. Hum. Reprod. 8:24-31(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=12545228;
RA   Ma Y.X., Zhang S.Z., Wu Q.Q., Sun Y.;
RT   "Cloning, expression and alternative splicing of a novel isoform of human
RT   TCP11b gene.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:182-188(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=12905703;
RA   Ma Y.X., Zhang S.Z., Wu Q.Q., Sun Y., Qiu W.M., Xu W.M.;
RT   "Cloning, expression, and alternative splicing of the novel isoform of
RT   hTCP11 gene.";
RL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 25:122-128(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5 AND 6), AND
RP   VARIANT ALA-253.
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., 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Brain, and Testis;
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   [8]
RP   INTERACTION WITH ODF1 (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY (ISOFORMS
RP   1; 2 AND 3).
RX   PubMed=21597245; DOI=10.1620/tjem.224.111;
RA   Liu Y., Jiang M., Li C., Yang P., Sun H., Tao D., Zhang S., Ma Y.;
RT   "Human t-complex protein 11 (TCP11), a testis-specific gene product, is a
RT   potential determinant of the sperm morphology.";
RL   Tohoku J. Exp. Med. 224:111-117(2011).
CC   -!- FUNCTION: Plays a role in the process of sperm capacitation and
CC       acrosome reactions. Probable receptor for the putative fertilization-
CC       promoting peptide (FPP) at the sperm membrane that may modulate the
CC       activity of the adenylyl cyclase cAMP pathway.
CC       {ECO:0000250|UniProtKB:Q01755}.
CC   -!- SUBUNIT: Found in a complex at least composed of MROH2B, PRKACA isoform
CC       2 and TCP11. Interacts with MROH2B. Interacts with PRKACA isoform 2 (By
CC       similarity). Isoform 2 and isoform 3 interact with ODF1 (via leucine
CC       zipper motif) (PubMed:21597245). {ECO:0000250|UniProtKB:Q01755,
CC       ECO:0000269|PubMed:21597245}.
CC   -!- INTERACTION:
CC       Q8WWU5-7; Q13155: AIMP2; NbExp=3; IntAct=EBI-17721485, EBI-745226;
CC       Q8WWU5-7; Q9NPI8: FANCF; NbExp=3; IntAct=EBI-17721485, EBI-81589;
CC       Q8WWU5-7; Q8TC17: GRAPL; NbExp=3; IntAct=EBI-17721485, EBI-18300553;
CC       Q8WWU5-7; O43708: GSTZ1; NbExp=3; IntAct=EBI-17721485, EBI-748043;
CC       Q8WWU5-7; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-17721485, EBI-10241252;
CC       Q8WWU5-7; Q9NUN5-4: LMBRD1; NbExp=3; IntAct=EBI-17721485, EBI-17721490;
CC       Q8WWU5-7; Q02750: MAP2K1; NbExp=3; IntAct=EBI-17721485, EBI-492564;
CC       Q8WWU5-7; Q9H204: MED28; NbExp=3; IntAct=EBI-17721485, EBI-514199;
CC       Q8WWU5-7; Q9GZQ6: NPFFR1; NbExp=3; IntAct=EBI-17721485, EBI-18212103;
CC       Q8WWU5-7; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-17721485, EBI-4395732;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:Q01755}. Cytoplasmic vesicle, secretory vesicle,
CC       acrosome {ECO:0000250|UniProtKB:Q01755}. Note=Localizes on the
CC       acrosomal cap region of acrosome-intact, but not acrosome-reacted
CC       sperm. Colocalizes with MROH2B and PRKACA on the acrosome and tail
CC       regions in round spermatids and spermatozoa regardless of the
CC       capacitation status of the sperm. {ECO:0000250|UniProtKB:Q01755}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1; Synonyms=TCP11b {ECO:0000303|PubMed:12545228};
CC         IsoId=Q8WWU5-1; Sequence=Displayed;
CC       Name=2; Synonyms=TCP11a {ECO:0000303|PubMed:21597245};
CC         IsoId=Q8WWU5-2; Sequence=VSP_032186;
CC       Name=3; Synonyms=TCP11c {ECO:0000303|PubMed:12905703};
CC         IsoId=Q8WWU5-3; Sequence=VSP_032185;
CC       Name=4;
CC         IsoId=Q8WWU5-4; Sequence=VSP_045217;
CC       Name=5;
CC         IsoId=Q8WWU5-5; Sequence=VSP_047125, VSP_047126;
CC       Name=6;
CC         IsoId=Q8WWU5-6; Sequence=VSP_047124;
CC       Name=7;
CC         IsoId=Q8WWU5-7; Sequence=VSP_047125;
CC   -!- TISSUE SPECIFICITY: Isoform 2 and isoform 3 are expressed in sperm.
CC       Isoform 1 is not detected in sperm (at protein level)
CC       (PubMed:21597245). Testis-specific (PubMed:11756566). Isoform 1,
CC       isoform 2 and isoform 3 are expressed in sperm (PubMed:21597245).
CC       {ECO:0000269|PubMed:11756566, ECO:0000269|PubMed:21597245}.
CC   -!- PTM: Constitutively phosphorylated on serine, threonine and tyrosine
CC       residues within the head and tail regions of noncapacitated
CC       spermatozoa. Phosphorylation on tyrosine residues increases upon sperm
CC       capacitation within the acrosomal region in a protein kinase A (PKA)-
CC       dependent signaling pathway. {ECO:0000250|UniProtKB:Q01755}.
CC   -!- SIMILARITY: Belongs to the TCP11 family. {ECO:0000305}.
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DR   EMBL; AF269223; AAF75551.1; -; mRNA.
DR   EMBL; AY069943; AAL58042.1; -; mRNA.
DR   EMBL; AF260330; AAF91370.1; -; mRNA.
DR   EMBL; AF536532; AAN04044.1; -; mRNA.
DR   EMBL; AF536533; AAN04045.1; -; mRNA.
DR   EMBL; AK057234; BAG51889.1; -; mRNA.
DR   EMBL; AK301975; BAH13597.1; -; mRNA.
DR   EMBL; AK315078; BAG37546.1; -; mRNA.
DR   EMBL; AK301778; BAH13551.1; -; mRNA.
DR   EMBL; AK302022; BAH13610.1; -; mRNA.
DR   EMBL; AK302456; BAH13714.1; -; mRNA.
DR   EMBL; AL138721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03808.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03809.1; -; Genomic_DNA.
DR   EMBL; BC033729; AAH33729.1; -; mRNA.
DR   EMBL; BC040003; AAH40003.1; -; mRNA.
DR   EMBL; BC048418; AAH48418.1; -; mRNA.
DR   EMBL; BC090050; AAH90050.1; -; mRNA.
DR   CCDS; CCDS47413.1; -. [Q8WWU5-1]
DR   CCDS; CCDS4799.1; -. [Q8WWU5-2]
DR   CCDS; CCDS59015.1; -. [Q8WWU5-3]
DR   CCDS; CCDS59016.1; -. [Q8WWU5-6]
DR   CCDS; CCDS59017.1; -. [Q8WWU5-4]
DR   RefSeq; NP_001087197.1; NM_001093728.2.
DR   RefSeq; NP_001248746.1; NM_001261817.1.
DR   RefSeq; NP_001248747.1; NM_001261818.1. [Q8WWU5-4]
DR   RefSeq; NP_001248748.1; NM_001261819.1. [Q8WWU5-6]
DR   RefSeq; NP_001248749.1; NM_001261820.1. [Q8WWU5-3]
DR   RefSeq; NP_001248750.1; NM_001261821.1. [Q8WWU5-3]
DR   RefSeq; NP_061149.1; NM_018679.5. [Q8WWU5-2]
DR   AlphaFoldDB; Q8WWU5; -.
DR   BioGRID; 112814; 13.
DR   IntAct; Q8WWU5; 12.
DR   STRING; 9606.ENSP00000308708; -.
DR   iPTMnet; Q8WWU5; -.
DR   PhosphoSitePlus; Q8WWU5; -.
DR   BioMuta; TCP11; -.
DR   DMDM; 74716246; -.
DR   jPOST; Q8WWU5; -.
DR   MassIVE; Q8WWU5; -.
DR   PaxDb; Q8WWU5; -.
DR   PeptideAtlas; Q8WWU5; -.
DR   PRIDE; Q8WWU5; -.
DR   ProteomicsDB; 17272; -.
DR   ProteomicsDB; 6850; -.
DR   ProteomicsDB; 6866; -.
DR   ProteomicsDB; 74933; -. [Q8WWU5-1]
DR   ProteomicsDB; 74934; -. [Q8WWU5-2]
DR   ProteomicsDB; 74935; -. [Q8WWU5-3]
DR   TopDownProteomics; Q8WWU5-2; -. [Q8WWU5-2]
DR   Antibodypedia; 29446; 100 antibodies from 21 providers.
DR   DNASU; 6954; -.
DR   Ensembl; ENST00000244645.7; ENSP00000244645.3; ENSG00000124678.20. [Q8WWU5-2]
DR   Ensembl; ENST00000311875.11; ENSP00000308708.6; ENSG00000124678.20. [Q8WWU5-1]
DR   Ensembl; ENST00000373974.8; ENSP00000363085.4; ENSG00000124678.20. [Q8WWU5-4]
DR   Ensembl; ENST00000373979.6; ENSP00000363091.2; ENSG00000124678.20. [Q8WWU5-2]
DR   Ensembl; ENST00000412155.6; ENSP00000402816.2; ENSG00000124678.20. [Q8WWU5-6]
DR   Ensembl; ENST00000418521.6; ENSP00000415320.2; ENSG00000124678.20. [Q8WWU5-3]
DR   Ensembl; ENST00000512012.5; ENSP00000425995.1; ENSG00000124678.20. [Q8WWU5-1]
DR   Ensembl; ENST00000611141.4; ENSP00000478603.1; ENSG00000124678.20. [Q8WWU5-3]
DR   Ensembl; ENST00000673754.1; ENSP00000501201.1; ENSG00000124678.20. [Q8WWU5-7]
DR   GeneID; 6954; -.
DR   KEGG; hsa:6954; -.
DR   MANE-Select; ENST00000311875.11; ENSP00000308708.6; NM_001370687.1; NP_001357616.1.
DR   UCSC; uc003ojz.3; human. [Q8WWU5-1]
DR   CTD; 6954; -.
DR   DisGeNET; 6954; -.
DR   GeneCards; TCP11; -.
DR   HGNC; HGNC:11658; TCP11.
DR   HPA; ENSG00000124678; Tissue enriched (testis).
DR   MIM; 186982; gene.
DR   neXtProt; NX_Q8WWU5; -.
DR   OpenTargets; ENSG00000124678; -.
DR   PharmGKB; PA36409; -.
DR   VEuPathDB; HostDB:ENSG00000124678; -.
DR   eggNOG; KOG1981; Eukaryota.
DR   GeneTree; ENSGT00940000161869; -.
DR   HOGENOM; CLU_026469_0_0_1; -.
DR   InParanoid; Q8WWU5; -.
DR   OMA; NQKVFGP; -.
DR   PhylomeDB; Q8WWU5; -.
DR   TreeFam; TF313385; -.
DR   PathwayCommons; Q8WWU5; -.
DR   SignaLink; Q8WWU5; -.
DR   BioGRID-ORCS; 6954; 7 hits in 1061 CRISPR screens.
DR   GeneWiki; TCP11; -.
DR   GenomeRNAi; 6954; -.
DR   Pharos; Q8WWU5; Tbio.
DR   PRO; PR:Q8WWU5; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8WWU5; protein.
DR   Bgee; ENSG00000124678; Expressed in sperm and 102 other tissues.
DR   ExpressionAtlas; Q8WWU5; baseline and differential.
DR   Genevisible; Q8WWU5; HS.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007281; P:germ cell development; IEP:UniProtKB.
DR   GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR   GO; GO:1902490; P:regulation of sperm capacitation; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR008862; Tcp11.
DR   PANTHER; PTHR12832; PTHR12832; 1.
DR   Pfam; PF05794; Tcp11; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasmic vesicle;
KW   Developmental protein; Differentiation; Flagellum; Membrane;
KW   Reference proteome; Spermatogenesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..503
FT                   /note="T-complex protein 11 homolog"
FT                   /id="PRO_0000324298"
FT   TRANSMEM        330..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..78
FT                   /note="MPDVKESVPPKYPGDSEGRSCKPETSGPPQEDKSGSEDPPPFLSVTGLTETV
FT                   NEVSKLSNKIGMNCDYYMEEKVLPPS -> MAPKGILGSFPTAMNL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:11756566,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032186"
FT   VAR_SEQ         1..63
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12905703,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032185"
FT   VAR_SEQ         1..46
FT                   /note="MPDVKESVPPKYPGDSEGRSCKPETSGPPQEDKSGSEDPPPFLSVT -> MT
FT                   RGGGGG (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047124"
FT   VAR_SEQ         1..42
FT                   /note="MPDVKESVPPKYPGDSEGRSCKPETSGPPQEDKSGSEDPPPF -> MTRGGG
FT                   GGV (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045217"
FT   VAR_SEQ         1
FT                   /note="M -> MTRGGGGGDTISKM (in isoform 5 and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047125"
FT   VAR_SEQ         42..47
FT                   /note="FLSVTG -> C (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047126"
FT   VARIANT         253
FT                   /note="G -> A (in dbSNP:rs2234045)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_039692"
FT   VARIANT         429
FT                   /note="R -> Q (in dbSNP:rs2234051)"
FT                   /id="VAR_039693"
FT   CONFLICT        157
FT                   /note="L -> R (in Ref. 4; BAH13714)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  56141 MW;  F567492970A3F68B CRC64;
     MPDVKESVPP KYPGDSEGRS CKPETSGPPQ EDKSGSEDPP PFLSVTGLTE TVNEVSKLSN
     KIGMNCDYYM EEKVLPPSSL EGKVKETVHN AFWDHLKEQL SATPPDFSCA LELLKEIKEI
     LLSLLLPRQN RLRIEIEEAL DMDLLKQEAE HGALKVLYLS KYVLNMMALL CAPVRDEAVQ
     KLENITDPVW LLRGIFQVLG RMKMDMVNYT IQSLQPHLQE HSIQYERAKF QELLNKQPSL
     LNHTTKWLTQ AAGDLTMSPP TCPDTSDSSS VAGPSPNEAA NNPEPLSPTM VLCQGFLNLL
     LWDLENEEFP ETLLMDRTRL QELKSQLHQL TVMASVLLVA SSFSGSVLFG SPQFVDKLKR
     ITKSLLEDFH SRPEEAILTV SEQVSQEIHQ SLKNMGLVAL SSDNTASLMG QLQNIAKKEN
     CVCSVIDQRI HLFLKCCLVL GVQRSLLDLP GGLTLIEAEL AELGQKFVNL THHNQQVFGP
     YYTEILKTLI SPAQALETKV ESV
 
 
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