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SYNE4_HUMAN
ID   SYNE4_HUMAN             Reviewed;         404 AA.
AC   Q8N205; A8MRS0; A8MYE3; Q7Z7L3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Nesprin-4;
DE   AltName: Full=KASH domain-containing protein 4;
DE            Short=KASH4;
DE   AltName: Full=Nuclear envelope spectrin repeat protein 4;
GN   Name=SYNE4; Synonyms=C19orf46;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT HIS-278.
RC   TISSUE=Mammary carcinoma;
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   [4]
RP   INVOLVEMENT IN DFNB76, AND SUBCELLULAR LOCATION.
RX   PubMed=23348741; DOI=10.1172/jci66911;
RA   Horn H.F., Brownstein Z., Lenz D.R., Shivatzki S., Dror A.A.,
RA   Dagan-Rosenfeld O., Friedman L.M., Roux K.J., Kozlov S., Jeang K.T.,
RA   Frydman M., Burke B., Stewart C.L., Avraham K.B.;
RT   "The LINC complex is essential for hearing.";
RL   J. Clin. Invest. 123:740-750(2013).
CC   -!- FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and
CC       Cytoskeleton) complex, involved in the connection between the nuclear
CC       lamina and the cytoskeleton. The nucleocytoplasmic interactions
CC       established by the LINC complex play an important role in the
CC       transmission of mechanical forces across the nuclear envelope and in
CC       nuclear movement and positioning (By similarity). Behaves as a kinesin
CC       cargo, providing a functional binding site for kinesin-1 at the nuclear
CC       envelope. Hence may contribute to the establishment of secretory
CC       epithelial morphology by promoting kinesin-dependent apical migration
CC       of the centrosome and Golgi apparatus and basal localization of the
CC       nucleus (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Core component of LINC complexes which are composed of inner
CC       nuclear membrane SUN domain-containing proteins coupled to outer
CC       nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC       containing proteins seem to bind each other promiscuously; however,
CC       differentially expression of LINC complex constituents can give rise to
CC       specific assemblies (By similarity). Probably part of a SUN1-containing
CC       LINC complex. Interacts with kinesins KIF5B and KLC1 (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8N205; Q9ULW3: ABT1; NbExp=3; IntAct=EBI-7131783, EBI-2602396;
CC       Q8N205; A8K660: ADIPOQ; NbExp=3; IntAct=EBI-7131783, EBI-10174479;
CC       Q8N205; Q6PL45: BRICD5; NbExp=3; IntAct=EBI-7131783, EBI-10254180;
CC       Q8N205; Q08722: CD47; NbExp=3; IntAct=EBI-7131783, EBI-1268321;
CC       Q8N205; Q96LK0: CEP19; NbExp=3; IntAct=EBI-7131783, EBI-741885;
CC       Q8N205; O95471: CLDN7; NbExp=3; IntAct=EBI-7131783, EBI-740744;
CC       Q8N205; P56748: CLDN8; NbExp=3; IntAct=EBI-7131783, EBI-10215641;
CC       Q8N205; Q9BXN2: CLEC7A; NbExp=7; IntAct=EBI-7131783, EBI-3939278;
CC       Q8N205; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-7131783, EBI-2548702;
CC       Q8N205; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-7131783, EBI-10267100;
CC       Q8N205; Q07325: CXCL9; NbExp=3; IntAct=EBI-7131783, EBI-3911467;
CC       Q8N205; Q5J5C9: DEFB121; NbExp=3; IntAct=EBI-7131783, EBI-10244198;
CC       Q8N205; O60344: ECE2; NbExp=3; IntAct=EBI-7131783, EBI-3906484;
CC       Q8N205; P56851: EDDM3B; NbExp=3; IntAct=EBI-7131783, EBI-10215665;
CC       Q8N205; P54849: EMP1; NbExp=3; IntAct=EBI-7131783, EBI-4319440;
CC       Q8N205; O75355: ENTPD3; NbExp=3; IntAct=EBI-7131783, EBI-10187968;
CC       Q8N205; Q96D05: FAM241B; NbExp=3; IntAct=EBI-7131783, EBI-2548784;
CC       Q8N205; Q969F0: FATE1; NbExp=5; IntAct=EBI-7131783, EBI-743099;
CC       Q8N205; Q9Y287: ITM2B; NbExp=3; IntAct=EBI-7131783, EBI-2866431;
CC       Q8N205; Q9NSK0: KLC4; NbExp=3; IntAct=EBI-7131783, EBI-949319;
CC       Q8N205; Q53G59: KLHL12; NbExp=3; IntAct=EBI-7131783, EBI-740929;
CC       Q8N205; Q96E93: KLRG1; NbExp=3; IntAct=EBI-7131783, EBI-750770;
CC       Q8N205; Q86UP2: KTN1; NbExp=3; IntAct=EBI-7131783, EBI-359761;
CC       Q8N205; Q13021: MALL; NbExp=3; IntAct=EBI-7131783, EBI-750078;
CC       Q8N205; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-7131783, EBI-10317612;
CC       Q8N205; Q16625: OCLN; NbExp=3; IntAct=EBI-7131783, EBI-2903088;
CC       Q8N205; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-7131783, EBI-2804156;
CC       Q8N205; Q8TBU1: OSTCL; NbExp=3; IntAct=EBI-7131783, EBI-10273677;
CC       Q8N205; Q9NXK6: PAQR5; NbExp=3; IntAct=EBI-7131783, EBI-10316423;
CC       Q8N205; Q5TAB7: RIPPLY2; NbExp=3; IntAct=EBI-7131783, EBI-10246897;
CC       Q8N205; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-7131783, EBI-8652744;
CC       Q8N205; Q15437: SEC23B; NbExp=3; IntAct=EBI-7131783, EBI-742673;
CC       Q8N205; Q9HC62: SENP2; NbExp=3; IntAct=EBI-7131783, EBI-714881;
CC       Q8N205; P11686: SFTPC; NbExp=3; IntAct=EBI-7131783, EBI-10197617;
CC       Q8N205; O00631: SLN; NbExp=3; IntAct=EBI-7131783, EBI-10180786;
CC       Q8N205; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-7131783, EBI-8640191;
CC       Q8N205; Q12893: TMEM115; NbExp=3; IntAct=EBI-7131783, EBI-8633987;
CC       Q8N205; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-7131783, EBI-2844246;
CC       Q8N205; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-7131783, EBI-348587;
CC       Q8N205; Q6ZP80: TMEM182; NbExp=3; IntAct=EBI-7131783, EBI-10255122;
CC       Q8N205; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-7131783, EBI-10314986;
CC       Q8N205; Q9NRS4-3: TMPRSS4; NbExp=3; IntAct=EBI-7131783, EBI-10312990;
CC       Q8N205; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-7131783, EBI-749955;
CC       Q8N205; O95858: TSPAN15; NbExp=3; IntAct=EBI-7131783, EBI-7361096;
CC       Q8N205; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-7131783, EBI-10243654;
CC       Q8N205; Q9UEU0: VTI1B; NbExp=4; IntAct=EBI-7131783, EBI-723716;
CC       Q8N205; P15622-3: ZNF250; NbExp=3; IntAct=EBI-7131783, EBI-10177272;
CC       Q8N205-2; Q15848: ADIPOQ; NbExp=6; IntAct=EBI-12099160, EBI-10827839;
CC       Q8N205-2; Q96LK0: CEP19; NbExp=3; IntAct=EBI-12099160, EBI-741885;
CC       Q8N205-2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12099160, EBI-12256978;
CC       Q8N205-2; A0A0S2Z5K4: CSGALNACT2; NbExp=3; IntAct=EBI-12099160, EBI-16434756;
CC       Q8N205-2; P24593: IGFBP5; NbExp=3; IntAct=EBI-12099160, EBI-720480;
CC       Q8N205-2; Q13021: MALL; NbExp=3; IntAct=EBI-12099160, EBI-750078;
CC       Q8N205-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12099160, EBI-748974;
CC       Q8N205-2; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-12099160, EBI-11721828;
CC       Q8N205-2; P11686: SFTPC; NbExp=4; IntAct=EBI-12099160, EBI-10197617;
CC       Q8N205-2; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-12099160, EBI-8640191;
CC       Q8N205-2; Q15560: TCEA2; NbExp=3; IntAct=EBI-12099160, EBI-710310;
CC       Q8N205-2; Q5T619: ZNF648; NbExp=3; IntAct=EBI-12099160, EBI-11985915;
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC       {ECO:0000269|PubMed:23348741}; Single-pass type IV membrane protein
CC       {ECO:0000269|PubMed:23348741}. Note=Localization at the nucleus outer
CC       membrane requires the presence of SUN1. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N205-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N205-2; Sequence=VSP_028444;
CC   -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC       mediates the nuclear envelope targeting and is involved in the binding
CC       to SUN1 and SUN2 through recognition of their SUN domains.
CC       {ECO:0000250}.
CC   -!- PTM: The disulfid bond with SUN1 or SUN2 is required for stability of
CC       the respective LINC complex under tensile forces.
CC       {ECO:0000250|UniProtKB:Q8WXH0}.
CC   -!- DISEASE: Deafness, autosomal recessive, 76 (DFNB76) [MIM:615540]: A
CC       form of non-syndromic sensorineural deafness, a disorder resulting from
CC       damage to the neural receptors of the inner ear, the nerve pathways to
CC       the brain, or the area of the brain that receives sound information.
CC       DFNB76 affected individuals have onset of progressive high frequency
CC       hearing impairment between birth and 6 years of age. The hearing loss
CC       is severe at high frequencies by adulthood.
CC       {ECO:0000269|PubMed:23348741}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC04222.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AK093764; BAC04222.1; ALT_SEQ; mRNA.
DR   EMBL; AC002116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF038458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052573; AAH52573.1; -; mRNA.
DR   CCDS; CCDS42553.1; -. [Q8N205-1]
DR   CCDS; CCDS77285.1; -. [Q8N205-2]
DR   RefSeq; NP_001034965.1; NM_001039876.2. [Q8N205-1]
DR   RefSeq; NP_001284664.1; NM_001297735.2. [Q8N205-2]
DR   PDB; 6R16; X-ray; 2.75 A; G/H/I/J/K/L=376-404.
DR   PDB; 6WMD; X-ray; 1.50 A; B=377-404.
DR   PDBsum; 6R16; -.
DR   PDBsum; 6WMD; -.
DR   AlphaFoldDB; Q8N205; -.
DR   SASBDB; Q8N205; -.
DR   SMR; Q8N205; -.
DR   BioGRID; 127856; 98.
DR   IntAct; Q8N205; 90.
DR   MINT; Q8N205; -.
DR   STRING; 9606.ENSP00000316130; -.
DR   iPTMnet; Q8N205; -.
DR   PhosphoSitePlus; Q8N205; -.
DR   BioMuta; SYNE4; -.
DR   DMDM; 158706458; -.
DR   EPD; Q8N205; -.
DR   jPOST; Q8N205; -.
DR   MassIVE; Q8N205; -.
DR   MaxQB; Q8N205; -.
DR   PaxDb; Q8N205; -.
DR   PeptideAtlas; Q8N205; -.
DR   PRIDE; Q8N205; -.
DR   ProteomicsDB; 71647; -. [Q8N205-1]
DR   ProteomicsDB; 71648; -. [Q8N205-2]
DR   Antibodypedia; 34811; 103 antibodies from 18 providers.
DR   DNASU; 163183; -.
DR   Ensembl; ENST00000324444.9; ENSP00000316130.3; ENSG00000181392.17. [Q8N205-1]
DR   Ensembl; ENST00000340477.9; ENSP00000343152.5; ENSG00000181392.17. [Q8N205-2]
DR   GeneID; 163183; -.
DR   KEGG; hsa:163183; -.
DR   MANE-Select; ENST00000324444.9; ENSP00000316130.3; NM_001039876.3; NP_001034965.1.
DR   UCSC; uc002ocq.2; human. [Q8N205-1]
DR   CTD; 163183; -.
DR   DisGeNET; 163183; -.
DR   GeneCards; SYNE4; -.
DR   HGNC; HGNC:26703; SYNE4.
DR   HPA; ENSG00000181392; Low tissue specificity.
DR   MalaCards; SYNE4; -.
DR   MIM; 615535; gene.
DR   MIM; 615540; phenotype.
DR   neXtProt; NX_Q8N205; -.
DR   OpenTargets; ENSG00000181392; -.
DR   Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR   PharmGKB; PA145149542; -.
DR   VEuPathDB; HostDB:ENSG00000181392; -.
DR   eggNOG; ENOG502SZGW; Eukaryota.
DR   GeneTree; ENSGT00510000049061; -.
DR   HOGENOM; CLU_034166_1_0_1; -.
DR   InParanoid; Q8N205; -.
DR   OMA; IRSEQAQ; -.
DR   OrthoDB; 938875at2759; -.
DR   PhylomeDB; Q8N205; -.
DR   PathwayCommons; Q8N205; -.
DR   SignaLink; Q8N205; -.
DR   SIGNOR; Q8N205; -.
DR   BioGRID-ORCS; 163183; 15 hits in 1074 CRISPR screens.
DR   ChiTaRS; SYNE4; human.
DR   GenomeRNAi; 163183; -.
DR   Pharos; Q8N205; Tbio.
DR   PRO; PR:Q8N205; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8N205; protein.
DR   Bgee; ENSG00000181392; Expressed in pancreatic ductal cell and 116 other tissues.
DR   ExpressionAtlas; Q8N205; baseline and differential.
DR   Genevisible; Q8N205; HS.
DR   GO; GO:0031309; C:integral component of nuclear outer membrane; ISS:UniProtKB.
DR   GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IEA:InterPro.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR   InterPro; IPR012315; KASH.
DR   InterPro; IPR030268; SYNE4.
DR   PANTHER; PTHR21640; PTHR21640; 1.
DR   Pfam; PF10541; KASH; 1.
DR   SMART; SM01249; KASH; 1.
DR   PROSITE; PS51049; KASH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Deafness; Disulfide bond; Membrane;
KW   Non-syndromic deafness; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..404
FT                   /note="Nesprin-4"
FT                   /id="PRO_0000306264"
FT   TOPO_DOM        1..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT   TRANSMEM        356..376
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT   TOPO_DOM        377..404
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT   DOMAIN          347..404
FT                   /note="KASH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        381
FT                   /note="Interchain (with C-563 in SUN2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT   DISULFID        381
FT                   /note="Interchain (with C-657 in SUN1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT   VAR_SEQ         94..206
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028444"
FT   VARIANT         224
FT                   /note="S -> L (in dbSNP:rs34818970)"
FT                   /id="VAR_035284"
FT   VARIANT         278
FT                   /note="Q -> H (in dbSNP:rs2285422)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_035285"
FT   STRAND          394..397
FT                   /evidence="ECO:0007829|PDB:6WMD"
SQ   SEQUENCE   404 AA;  43512 MW;  F15E209FB06636D2 CRC64;
     MALSLPLGPR LGSEPLNHPP GAPREADIVG CTVCPASGEE STSPEQAQTL GQDSLGPPEH
     FQGGPRGNEP AAHPPRWSTP SSYEDPAGGK HCEHPISGLE VLEAEQNSLH LCLLGLGRRL
     QDLEQGLGHW ALAQSGMVQL QALQVDLRGA AERVEALLAF GEGLAQRSEP RAWAALEQIL
     RALGAYRDSI FRRLWQLQAQ LVSYSLVFEE ANTLDQDLEV EGDSDWPGPG GVWGPWAPSS
     LPTSTELEWD PAGDIGGLGP LGQKTARTLG VPCELCGQRG PQGRGQGLEE ADTSHSRQDM
     LESGLGHQKR LARHQRHSLL RKPQDKKRQA SPHLQDVRLE GNPGAPDPAS RQPLTFLLIL
     FLLFLLLVGA MFLLPASGGP CCSHARIPRT PYLVLSYVNG LPPV
 
 
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