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SDK1_HUMAN
ID   SDK1_HUMAN              Reviewed;        2213 AA.
AC   Q7Z5N4; Q8TEN9; Q8TEP5; Q96N44;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Protein sidekick-1 {ECO:0000303|PubMed:15213259};
DE   Flags: Precursor;
GN   Name=SDK1 {ECO:0000303|PubMed:15213259, ECO:0000312|HGNC:HGNC:19307};
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).
RC   TISSUE=Brain;
RA   Bonner T.I.;
RT   "Complete coding sequence of human sidekick homolog 1.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-2213 (ISOFORM 3), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1642-2213 (ISOFORM 1), AND VARIANTS ASN-1016
RP   AND ARG-1641.
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15213259; DOI=10.1097/01.asn.0000128975.28958.c2;
RA   Kaufman L., Hayashi K., Ross M.J., Ross M.D., Klotman P.E.;
RT   "Sidekick-1 is upregulated in glomeruli in HIV-associated nephropathy.";
RL   J. Am. Soc. Nephrol. 15:1721-1730(2004).
CC   -!- FUNCTION: Adhesion molecule that promotes lamina-specific synaptic
CC       connections in the retina. Expressed in specific subsets of
CC       interneurons and retinal ganglion cells (RGCs) and promotes synaptic
CC       connectivity via homophilic interactions.
CC       {ECO:0000250|UniProtKB:Q8AV58}.
CC   -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC       adhesion. {ECO:0000250|UniProtKB:Q8AV58}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8AV58};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV58}.
CC       Synapse {ECO:0000250|UniProtKB:Q8AV58}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7Z5N4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z5N4-2; Sequence=VSP_017517, VSP_017519;
CC       Name=3;
CC         IsoId=Q7Z5N4-3; Sequence=VSP_017518;
CC   -!- TISSUE SPECIFICITY: Up-regulated in glomeruli in HIV-associated
CC       nephropathy. In diseased glomeruli, significantly overexpressed and the
CC       expression is no longer restricted to mesangial cells but includes
CC       podocytes and parietal epithelial cells (PubMed:15213259).
CC       {ECO:0000269|PubMed:15213259}.
CC   -!- DOMAIN: Ig-like C2-type domains 1 and 2 mediate homophilic
CC       interactions. {ECO:0000250|UniProtKB:Q3UH53}.
CC   -!- MISCELLANEOUS: Dysregulation of this protein may play an important role
CC       in podocyte dysfunction in HIV-associated nephropathy.
CC       {ECO:0000269|PubMed:15213259}.
CC   -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
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DR   EMBL; AY310398; AAP75619.1; -; mRNA.
DR   EMBL; AK055987; BAB71066.1; -; mRNA.
DR   EMBL; AC004935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC004984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC015968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK074077; BAB84903.1; -; mRNA.
DR   EMBL; AK074083; BAB84909.1; -; mRNA.
DR   CCDS; CCDS34590.1; -. [Q7Z5N4-1]
DR   RefSeq; NP_689957.3; NM_152744.3. [Q7Z5N4-1]
DR   AlphaFoldDB; Q7Z5N4; -.
DR   SMR; Q7Z5N4; -.
DR   BioGRID; 128768; 20.
DR   IntAct; Q7Z5N4; 5.
DR   MINT; Q7Z5N4; -.
DR   STRING; 9606.ENSP00000385899; -.
DR   CarbonylDB; Q7Z5N4; -.
DR   GlyGen; Q7Z5N4; 19 sites.
DR   iPTMnet; Q7Z5N4; -.
DR   PhosphoSitePlus; Q7Z5N4; -.
DR   BioMuta; SDK1; -.
DR   DMDM; 296452965; -.
DR   jPOST; Q7Z5N4; -.
DR   MassIVE; Q7Z5N4; -.
DR   PaxDb; Q7Z5N4; -.
DR   PeptideAtlas; Q7Z5N4; -.
DR   PRIDE; Q7Z5N4; -.
DR   ProteomicsDB; 69335; -. [Q7Z5N4-1]
DR   ProteomicsDB; 69336; -. [Q7Z5N4-2]
DR   ProteomicsDB; 69337; -. [Q7Z5N4-3]
DR   Antibodypedia; 2506; 32 antibodies from 16 providers.
DR   DNASU; 221935; -.
DR   Ensembl; ENST00000404826.7; ENSP00000385899.2; ENSG00000146555.20. [Q7Z5N4-1]
DR   GeneID; 221935; -.
DR   KEGG; hsa:221935; -.
DR   MANE-Select; ENST00000404826.7; ENSP00000385899.2; NM_152744.4; NP_689957.3.
DR   UCSC; uc003smx.4; human. [Q7Z5N4-1]
DR   CTD; 221935; -.
DR   DisGeNET; 221935; -.
DR   GeneCards; SDK1; -.
DR   HGNC; HGNC:19307; SDK1.
DR   HPA; ENSG00000146555; Tissue enhanced (pancreas).
DR   MIM; 607216; gene.
DR   neXtProt; NX_Q7Z5N4; -.
DR   OpenTargets; ENSG00000146555; -.
DR   PharmGKB; PA134957188; -.
DR   VEuPathDB; HostDB:ENSG00000146555; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000157747; -.
DR   InParanoid; Q7Z5N4; -.
DR   OMA; NWKRNGV; -.
DR   OrthoDB; 134749at2759; -.
DR   PhylomeDB; Q7Z5N4; -.
DR   TreeFam; TF316846; -.
DR   PathwayCommons; Q7Z5N4; -.
DR   Reactome; R-HSA-373756; SDK interactions.
DR   SignaLink; Q7Z5N4; -.
DR   BioGRID-ORCS; 221935; 12 hits in 1062 CRISPR screens.
DR   ChiTaRS; SDK1; human.
DR   GenomeRNAi; 221935; -.
DR   Pharos; Q7Z5N4; Tbio.
DR   PRO; PR:Q7Z5N4; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q7Z5N4; protein.
DR   Bgee; ENSG00000146555; Expressed in popliteal artery and 117 other tissues.
DR   ExpressionAtlas; Q7Z5N4; baseline and differential.
DR   Genevisible; Q7Z5N4; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0060998; P:regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR   CDD; cd00063; FN3; 13.
DR   Gene3D; 2.60.40.10; -; 19.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF00041; fn3; 13.
DR   Pfam; PF07679; I-set; 3.
DR   SMART; SM00060; FN3; 13.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 6.
DR   SUPFAM; SSF48726; SSF48726; 6.
DR   SUPFAM; SSF49265; SSF49265; 7.
DR   PROSITE; PS50853; FN3; 13.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW   Signal; Synapse; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..2213
FT                   /note="Protein sidekick-1"
FT                   /id="PRO_0000226975"
FT   TOPO_DOM        ?..2009
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2010..2030
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2031..2213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          104..186
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          191..277
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          293..378
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          386..476
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          480..569
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          574..663
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          670..766
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          771..867
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          872..970
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          974..1068
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1072..1171
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1176..1274
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1279..1376
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1380..1474
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1479..1576
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1581..1699
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1704..1800
FT                   /note="Fibronectin type-III 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1804..1899
FT                   /note="Fibronectin type-III 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1902..2000
FT                   /note="Fibronectin type-III 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2075..2098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2207..2213
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q6V4S5"
FT   COMPBIAS        25..51
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        655
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        782
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        821
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        882
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1015
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1024
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1654
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1748
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1819
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1893
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        315..362
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        408..458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        501..553
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        595..647
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..1940
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_017517"
FT   VAR_SEQ         1643..1662
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_017518"
FT   VAR_SEQ         1941..1942
FT                   /note="PS -> ME (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_017519"
FT   VARIANT         1016
FT                   /note="D -> N (in dbSNP:rs11978101)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_025529"
FT   VARIANT         1641
FT                   /note="H -> R (in dbSNP:rs671694)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_025530"
FT   CONFLICT        58
FT                   /note="S -> P (in Ref. 1; AAP75619 and 2; BAB71066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="R -> H (in Ref. 1; AAP75619 and 2; BAB71066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        711
FT                   /note="N -> S (in Ref. 1; AAP75619 and 2; BAB71066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1666
FT                   /note="H -> D (in Ref. 4; BAB84909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2213 AA;  242112 MW;  7475FB659695F2C5 CRC64;
     MARGARPSAA GGGGGGAEPP ERAGPGRPRG SPPGRARPSL APRPGPEPSR PRAAPETSGG
     DTAGAGRCGG RRAAKLGPGR RGWWALLALQ LHLLRALAQD DVAPYFKTEP GLPQIHLEGN
     RLVLTCLAEG SWPLEFKWMR DDSELTTYSS EYKYIIPSLQ KLDAGFYRCV VRNRMGALLQ
     RKSEVQVAYM GSFMDTDQRK TVSQGRAAIL NLLPITSYPR PQVTWFREGH KIIPSNRIAI
     TLENQLVILA TTTSDAGAYY VQAVNEKNGE NKTSPFIHLS IARDVGTPET MAPTIVVPPG
     NRSVVAGSSE TTLECIASAR PVEDLSVTWK RNGVRITSGL HSFGRRLTIS NPTSADTGPY
     VCEAALPGSA FEPARATAFL FIIEPPYFTA EPESRISAEV EETVDIGCQA MGVPLPTLQW
     YKDAISISRL QNPRYKVLAS GGLRIQKLRP EDSGIFQCFA SNEGGEIQTH TYLDVTNIAP
     VFTQRPVDTT VTDGMTAILR CEVSGAPKPA ITWKRENHIL ASGSVRIPRF MLLESGGLQI
     APVFIQDAGN YTCYAANTEG SLNASATLTV WNRTSIVHPP EDHVVIKGTT ATLHCGATHD
     PRVSLRYVWK KDNVALTPSS TSRIVVEKDG SLLISQTWSG DIGDYSCEIV SEGGNDSRMA
     RLEVIELPHS PQNLLVSPNS SHSHAVVLSW VRPFDGNSPI LYYIVELSEN NSPWKVHLSN
     VGPEMTGVTV SGLTPARTYQ FRVCAVNEVG RGQYSAETSR LMLPEEPPSA PPKNIVASGR
     TNQSIMVQWQ PPPETEHNGV LRGYILRYRL AGLPGEYQQR NITSPEVNYC LVTDLIIWTQ
     YEIQVAAYNG AGLGVFSRAV TEYTLQGVPT APPQNVQTEA VNSTTIQFLW NPPPQQFING
     INQGYKLLAW PADAPEAVTV VTIAPDFHGV HHGHITNLKK FTAYFTSVLC FTTPGDGPPS
     TPQLVWTQED KPGAVGHLSF TEILDTSLKV SWQEPLEKNG IITGYQISWE VYGRNDSRLT
     HTLNSTTHEY KIQGLSSLTT YTIDVAAVTA VGTGLVTSST ISSGVPPDLP GAPSNLVISN
     ISPRSATLQF RPGYDGKTSI SRWIVEGQVG AIGDEEEWVT LYEEENEPDA QMLEIPNLTP
     YTHYRFRMKQ VNIVGPSPYS PSSRVIQTLQ APPDVAPTSV TVRTASETSL RLRWVPLPDS
     QYNGNPESVG YRIKYWRSDL QSSAVAQVVS DRLEREFTIE ELEEWMEYEL QMQAFNAVGA
     GPWSEVVRGR TRESVPSAAP ENVSAEAVSS TQILLTWTSV PEQDQNGLIL GYKILFRAKD
     LDPEPRSHIV RGNHTQSALL AGLRKFVLYE LQVLAFTRIG NGVPSTPLIL ERTKDDAPGP
     PVRLVFPEVR LTSVRIVWQP PEEPNGIILG YQIAYRLASS SPHTFTTVEV GATVRQFTAT
     DLAPESAYIF RLSAKTRQGW GEPLEATVIT TEKRERPAPP RELLVPQAEV TARSLRLQWV
     PGSDGASPIR YFTMQVRELP RGEWQTYSSS ISHEATACVV DRLRPFTSYK LRLKATNDIG
     DSDFSSETEA VTTLQDVPGE PPGSVSATPH TTSSVLIQWQ PPRDESLNGL LQGYRIYYRE
     LEYEAGSGTE AKTLKNPIAL HAELTAQSSF KTVNSSSTST MCELTHLKKY RRYEVIMTAY
     NIIGESPASA PVEVFVGEAA PAMAPQNVQV TPLTASQLEV TWDPPPPESQ NGNIQGYKIY
     YWEADSQNET EKMKVLFLPE PVVRLKNLTS HTKYLVSISA FNAAGDGPKS DPQQGRTHQA
     APGAPSFLAF SEITSTTLNV SWGEPAAANG ILQGYRVVYE PLAPVQGVSK VVTVEVRGNW
     QRWLKVRDLT KGVTYFFRVQ ARTITYGPEL QANITAGPAE GSPGSPRDVL VTKSASELTL
     QWTEGHSGDT PTTGYVIEAR PSDEGLWDMF VKDIPRSATS YTLSLDKLRQ GVTYEFRVVA
     VNEAGYGEPS NPSTAVSAQV EAPFYEEWWF LLVMALSSLI VILLVVFALV LHGQNKKYKN
     CSTGKGISTM EESVTLDNGG FAALELSSRH LNVKSTFSKK NGTRSPPRPS PGGLHYSDED
     ICNKYNGAVL TESVSLKEKS ADASESEATD SDYEDALPKH SFVNHYMSDP TYYNSWKRRA
     QGRAPAPHRY EAVAGSEAGA QLHPVITTQS AGGVYTPAGP GARTPLTGFS SFV
 
 
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