|SYNE3_HUMAN » Nesprin-3 » Nuclear envelope spectrin repeat protein 3;|
|Hydrophobic Thickness||30.0 ± 3.3 Å|
|Tilt Angle||12 ± 8°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC|
|TM Segments||927-948 (927-952)|
|UniProt annotation for SYNE3_HUMAN » Nesprin-3|
|FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow- induced centrosome polarization and directional migration in aortic endothelial cells. SUBUNIT: Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN domain-containing proteins interact with A-type lamins of the nuclear lamina, while at the other end of the complex, nesprins interact with unique cytoskeletal components. Interacts with PLEC (via actin-binding domain). Interacts with DST. Interacts with SYNE1 via spectrin repeats. Interacts (via KASH domain) with TOR1A (ATP-bound); the interaction is required for SYNE3 nuclear envelope localization. TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein level). DOMAIN: The KASH domain is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains.|
|UniProt features for SYNE3_HUMAN » Nesprin-3|
CHAIN 1 975 Nesprin-3. |
REPEAT 220 325 Spectrin 1.
REPEAT 647 740 Spectrin 2.
DOMAIN 917 975 KASH.
COILED 617 645 Potential.
|Amino Acid Sequence for SYNE3_HUMAN » Nesprin-3|
|MTQQPQDDFD RSVEDAQAWM KAVQDQLQVN DNTQGPRAAL EARLWETEKI CQLEPEGRVR VDLVLRMAEA LLACCPGDQK PGILARLKDI KAQWEETVTY MTHCHSRIEW VWLHWSEYLL ARDEFYRWFQ KMMVTLEPHI ELQLGLKEKQ WQLSHAQVLL HNVDNQAVLL DRLLEEAASL FNRIGDPSVD EDAQKRMKAE YDAVKAKAQK RVDLLEQVAR EHEEYQAGVD EFQLWLKAVV EKVNGCLGRN CKLPITQRLS TLQDIAKDFP RGEESLETLE EQSAGVIRNT SPLGAEKITG ELEEMRKVLE KLRALWEEEE ERLRGLLRSR GAWEQQIKQL EAELSEFRMV LQRLAQEGLQ PAAKAGTEDE LVAHWRRYSA TRAALASEEP RVDRLQAQLK ELIVFPHNLK PLSDSVIATI QEYQSLKVKS ARLRNAAAVE LWQHFQRPLQ DLQLWKALAQ RLLEVTASLP DLPSLHTFLP QIEAALMESS RLKELLTMLQ LKKDLLIGIF GQERATALLE QVAGSMRDRD LLHNSLLQRK SKLQSLLAQH KDFGAAFEPL QRKLLDLQVR VQAEKGLQRD LPGKQAQLSR LQGLQEEGLD LGAQMEAARP LVQENPNHQH KMDQLSSDFQ ALQRSLEDLV DRCRQSVQEH CTFSHQLLEL RQWIVVTTQK LEAHRGEAGP GDAESQEAEF ERLVAEFPEK EAQLSLVEAQ GWLVMEKSSP EGAAVVQEEL RELAESWRAL RLLEESLLSL IRNWHLQRME VDSGKKMVFT NNIPKSGFLI NPMDPIPRHR RRANLLQEEE GSHEDFSQLL RNFGQWLQVE NSKLVRIIAM RTSTAEDLRT RKSKLQELEA RVPEGQHLFE NLLRLGPARG TSDELEDLRY QWMLYKSKLK DSGHLLTQSS PGEPTGFQKT RRWRGLGSLF RRACCVALPL QLLLLLFLLL LFLLPIREED RSCTLANNFA RSFTLMLRYN GPPPT|