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SNP47_HUMAN
ID   SNP47_HUMAN             Reviewed;         464 AA.
AC   Q5SQN1; B6EDE0; Q5HYB5; Q5TBZ3; Q8N558; Q8TB31; Q8TCW8; Q8WV46; Q96CQ3;
AC   Q96FE1; Q96I66; Q96NU3; Q9BT10; Q9BVB2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Synaptosomal-associated protein 47;
DE            Short=SNAP-47;
DE   AltName: Full=Epididymis luminal protein 170;
DE   AltName: Full=Synaptosomal-associated 47 kDa protein;
GN   Name=SNAP47; Synonyms=C1orf142, HEL170, SVAP1;
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 1), AND VARIANT MET-154.
RA   Yang J., Qiu Y.;
RT   "Homo sapiens GRASP protein.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Colon endothelium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS
RP   ARG-119; MET-154 AND CYS-381.
RC   TISSUE=Cervix, Kidney, Lung, Muscle, Ovary, Pancreas, and Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-464 (ISOFORM 2), AND VARIANT
RP   CYS-381.
RC   TISSUE=Astrocyte;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-464 (ISOFORM 1).
RA   Li J., Wang H.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   ASSOCIATION WITH THE BLOC-1 COMPLEX, AND INTERACTION WITH BLOC1S6.
RX   PubMed=19546860; DOI=10.1038/mp.2009.58;
RA   Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
RA   Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
RA   Dell'Angelica E.C.;
RT   "The dysbindin-containing complex (BLOC-1) in brain: developmental
RT   regulation, interaction with SNARE proteins and role in neurite
RT   outgrowth.";
RL   Mol. Psychiatry 15:204-215(2010).
CC   -!- FUNCTION: Plays a role in intracellular membrane fusion. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex containing SNAP47, VAMP2 and STX1A (By
CC       similarity). Associates with the BLOC-1 complex. Interacts with
CC       BLOC1S6. {ECO:0000250, ECO:0000269|PubMed:19546860}.
CC   -!- INTERACTION:
CC       Q5SQN1; P55056: APOC4; NbExp=3; IntAct=EBI-10244848, EBI-18302142;
CC       Q5SQN1; P41181: AQP2; NbExp=3; IntAct=EBI-10244848, EBI-12701138;
CC       Q5SQN1; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-10244848, EBI-10181988;
CC       Q5SQN1; Q9Y624: F11R; NbExp=3; IntAct=EBI-10244848, EBI-742600;
CC       Q5SQN1; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10244848, EBI-10175124;
CC       Q5SQN1; Q969F0: FATE1; NbExp=3; IntAct=EBI-10244848, EBI-743099;
CC       Q5SQN1; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10244848, EBI-618309;
CC       Q5SQN1; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10244848, EBI-749265;
CC       Q5SQN1; Q6P597: KLC3; NbExp=3; IntAct=EBI-10244848, EBI-1643885;
CC       Q5SQN1; Q9H400: LIME1; NbExp=3; IntAct=EBI-10244848, EBI-2830566;
CC       Q5SQN1; Q9HCJ2: LRRC4C; NbExp=3; IntAct=EBI-10244848, EBI-3925442;
CC       Q5SQN1; P43360: MAGEA6; NbExp=3; IntAct=EBI-10244848, EBI-1045155;
CC       Q5SQN1; O14880: MGST3; NbExp=3; IntAct=EBI-10244848, EBI-724754;
CC       Q5SQN1; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-10244848, EBI-10172526;
CC       Q5SQN1; P15151: PVR; NbExp=3; IntAct=EBI-10244848, EBI-3919694;
CC       Q5SQN1; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-10244848, EBI-12055631;
CC       Q5SQN1; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10244848, EBI-3920694;
CC       Q5SQN1; Q96R06: SPAG5; NbExp=3; IntAct=EBI-10244848, EBI-413317;
CC       Q5SQN1; Q86Y82: STX12; NbExp=2; IntAct=EBI-10244848, EBI-2691717;
CC       Q5SQN1; Q16623: STX1A; NbExp=3; IntAct=EBI-10244848, EBI-712466;
CC       Q5SQN1; P61266: STX1B; NbExp=3; IntAct=EBI-10244848, EBI-9071709;
CC       Q5SQN1; Q12846: STX4; NbExp=3; IntAct=EBI-10244848, EBI-744942;
CC       Q5SQN1; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-10244848, EBI-10262539;
CC       Q5SQN1; O75379: VAMP4; NbExp=2; IntAct=EBI-10244848, EBI-744953;
CC       Q5SQN1; P51809: VAMP7; NbExp=4; IntAct=EBI-10244848, EBI-1052205;
CC       Q5SQN1; PRO_0000037316 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-10244848, EBI-25475825;
CC       Q5SQN1; P32851: Stx1a; Xeno; NbExp=3; IntAct=EBI-10244848, EBI-539720;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cytoplasm,
CC       perinuclear region {ECO:0000250}. Note=Appears to be exclusively
CC       membrane-bound. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SQN1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SQN1-2; Sequence=VSP_028614;
CC       Name=3;
CC         IsoId=Q5SQN1-3; Sequence=VSP_028613, VSP_028614;
CC       Name=4;
CC         IsoId=Q5SQN1-4; Sequence=VSP_028613;
CC   -!- SIMILARITY: Belongs to the SVAP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB70779.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY090635; AAM09082.1; -; mRNA.
DR   EMBL; BX648570; CAI45994.1; -; mRNA.
DR   EMBL; AL136378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL731702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471098; EAW69817.1; -; Genomic_DNA.
DR   EMBL; BC001332; AAH01332.1; -; mRNA.
DR   EMBL; BC004418; AAH04418.1; -; mRNA.
DR   EMBL; BC007786; AAH07786.2; -; mRNA.
DR   EMBL; BC011145; AAH11145.1; -; mRNA.
DR   EMBL; BC014059; AAH14059.2; -; mRNA.
DR   EMBL; BC018760; AAH18760.2; -; mRNA.
DR   EMBL; BC025231; AAH25231.1; -; mRNA.
DR   EMBL; BC032775; AAH32775.1; -; mRNA.
DR   EMBL; AK054633; BAB70779.1; ALT_INIT; mRNA.
DR   EMBL; FJ236305; ACI45237.1; -; mRNA.
DR   RefSeq; NP_001310864.1; NM_001323935.1. [Q5SQN1-2]
DR   RefSeq; NP_444280.2; NM_053052.3.
DR   RefSeq; XP_016855720.1; XM_017000231.1. [Q5SQN1-1]
DR   RefSeq; XP_016855721.1; XM_017000232.1. [Q5SQN1-1]
DR   AlphaFoldDB; Q5SQN1; -.
DR   SMR; Q5SQN1; -.
DR   BioGRID; 125534; 192.
DR   IntAct; Q5SQN1; 49.
DR   MINT; Q5SQN1; -.
DR   STRING; 9606.ENSP00000314157; -.
DR   GlyGen; Q5SQN1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5SQN1; -.
DR   PhosphoSitePlus; Q5SQN1; -.
DR   BioMuta; SNAP47; -.
DR   DMDM; 238054367; -.
DR   EPD; Q5SQN1; -.
DR   jPOST; Q5SQN1; -.
DR   MassIVE; Q5SQN1; -.
DR   MaxQB; Q5SQN1; -.
DR   PaxDb; Q5SQN1; -.
DR   PeptideAtlas; Q5SQN1; -.
DR   PRIDE; Q5SQN1; -.
DR   ProteomicsDB; 63811; -. [Q5SQN1-1]
DR   ProteomicsDB; 63812; -. [Q5SQN1-2]
DR   ProteomicsDB; 63813; -. [Q5SQN1-3]
DR   ProteomicsDB; 63814; -. [Q5SQN1-4]
DR   Antibodypedia; 34657; 45 antibodies from 17 providers.
DR   DNASU; 116841; -.
DR   Ensembl; ENST00000366760.5; ENSP00000355722.1; ENSG00000143740.15. [Q5SQN1-4]
DR   Ensembl; ENST00000418653.6; ENSP00000402730.2; ENSG00000143740.15. [Q5SQN1-3]
DR   Ensembl; ENST00000679561.1; ENSP00000504959.1; ENSG00000143740.15. [Q5SQN1-4]
DR   Ensembl; ENST00000680695.1; ENSP00000506091.1; ENSG00000143740.15. [Q5SQN1-4]
DR   Ensembl; ENST00000681929.1; ENSP00000505648.1; ENSG00000143740.15. [Q5SQN1-4]
DR   GeneID; 116841; -.
DR   KEGG; hsa:116841; -.
DR   UCSC; uc001hra.3; human. [Q5SQN1-1]
DR   CTD; 116841; -.
DR   DisGeNET; 116841; -.
DR   GeneCards; SNAP47; -.
DR   HGNC; HGNC:30669; SNAP47.
DR   HPA; ENSG00000143740; Low tissue specificity.
DR   MIM; 619659; gene.
DR   neXtProt; NX_Q5SQN1; -.
DR   OpenTargets; ENSG00000143740; -.
DR   PharmGKB; PA164725983; -.
DR   VEuPathDB; HostDB:ENSG00000143740; -.
DR   eggNOG; KOG3065; Eukaryota.
DR   GeneTree; ENSGT00950000182843; -.
DR   HOGENOM; CLU_1102480_0_0_1; -.
DR   InParanoid; Q5SQN1; -.
DR   OMA; FDNMMQG; -.
DR   OrthoDB; 662135at2759; -.
DR   PhylomeDB; Q5SQN1; -.
DR   TreeFam; TF331066; -.
DR   PathwayCommons; Q5SQN1; -.
DR   SignaLink; Q5SQN1; -.
DR   BioGRID-ORCS; 116841; 15 hits in 1089 CRISPR screens.
DR   ChiTaRS; SNAP47; human.
DR   GenomeRNAi; 116841; -.
DR   Pharos; Q5SQN1; Tdark.
DR   PRO; PR:Q5SQN1; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5SQN1; protein.
DR   Bgee; ENSG00000143740; Expressed in pancreatic ductal cell and 176 other tissues.
DR   ExpressionAtlas; Q5SQN1; baseline and differential.
DR   Genevisible; Q5SQN1; HS.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR   GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PROSITE; PS50192; T_SNARE; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane; Reference proteome;
KW   Repeat.
FT   CHAIN           1..464
FT                   /note="Synaptosomal-associated protein 47"
FT                   /id="PRO_0000307151"
FT   DOMAIN          154..216
FT                   /note="t-SNARE coiled-coil homology 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          401..463
FT                   /note="t-SNARE coiled-coil homology 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          20..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..242
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_028613"
FT   VAR_SEQ         417..464
FT                   /note="ILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKRLT ->
FT                   GFRPMSLSTQTVLVMLCSESAGALWRQRLS (in isoform 2 and isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_028614"
FT   VARIANT         48
FT                   /note="R -> G (in dbSNP:rs2236359)"
FT                   /id="VAR_035367"
FT   VARIANT         119
FT                   /note="G -> R (in dbSNP:rs12239037)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035368"
FT   VARIANT         154
FT                   /note="V -> M (in dbSNP:rs2236358)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT                   /id="VAR_035369"
FT   VARIANT         381
FT                   /note="R -> C (in dbSNP:rs17851681)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035370"
FT   CONFLICT        84..86
FT                   /note="DST -> TRP (in Ref. 5; AAH01332)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  52562 MW;  FC4061061B0042ED CRC64;
     MRAARRGLHC AGAERPRRRG RLWDSSGVPQ RQKRPGPWRT QTQEQMSRDV CIHTWPCTYY
     LEPKRRWVTG QLSLTSLSLR FMTDSTGEIL VSFPLSSIVE IKKEASHFIF SSITILEKGH
     AKHWFSSLRP SRNVVFSIIE HFWRELLLSQ PGAVADASVP RTRGEELTGL MAGSQKRLED
     TARVLHHQGQ QLDSVMRGLD KMESDLEVAD RLLTELESPA WWPFSSKLWK TPPETKPRED
     VSMTSCEPFG KEGILIKIPA VISHRTESHV KPGRLTVLVS GLEIHDSSSL LMHRFEREDV
     DDIKVHSPYE ISIRQRFIGK PDMAYRLISA KMPEVIPILE VQFSKKMELL EDALVLRSAR
     TSSPAEKSCS VWHAASGLMG RTLHREPPAG DQEGTALHLQ TSLPALSEAD TQELTQILRR
     MKGLALEAES ELERQDEALD GVAAAVDRAT LTIDKHNRRM KRLT
 
 
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