VINC_OSCPE
ID VINC_OSCPE Reviewed; 846 AA.
AC A0A3B6UES5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Vinculin {ECO:0000303|PubMed:29880641};
GN Name=VIN1 {ECO:0000312|EMBL:AYN71345.1};
OS Oscarella pearsei (Sponge).
OC Eukaryota; Metazoa; Porifera; Homoscleromorpha; Homosclerophorida;
OC Oscarellidae; Oscarella.
OX NCBI_TaxID=1940113;
RN [1] {ECO:0007744|PDB:6BFI}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS),
RP FUNCTION, SUBUNIT, INTERACTION WITH TLN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=29880641; DOI=10.1074/jbc.ra117.001325;
RA Miller P.W., Pokutta S., Mitchell J.M., Chodaparambil J.V., Clarke D.N.,
RA Nelson W.J., Weis W.I., Nichols S.A.;
RT "Analysis of a vinculin homolog in a sponge (phylum Porifera) reveals that
RT vertebrate-like cell adhesions emerged early in animal evolution.";
RL J. Biol. Chem. 293:11674-11686(2018).
CC -!- FUNCTION: Actin filament (F-actin)-binding protein which may play a
CC role in cell-cell adhesion. {ECO:0000269|PubMed:29880641}.
CC -!- SUBUNIT: Monomer. Interacts with TLN (talin); the interaction
CC facilitates VIN1 binding to F-actin. {ECO:0000269|PubMed:29880641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:29880641}. Cell projection, filopodium
CC {ECO:0000269|PubMed:29880641}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:29880641}. Note=Localizes to points of cell-cell
CC contact in the pinacoderm. Localizes to the base of the microvillar
CC collar in choanocytes. Detected in filopodial extensions in migratory
CC cells of the mesohyl. Colocalizes with F-actin.
CC {ECO:0000269|PubMed:29880641}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial tissues, specifically the
CC pinacoderm (outer epithelium) and choanoderm (feeding epithelium) (at
CC protein level). Also detected in migratory cells of the mesohyl (at
CC protein level). {ECO:0000269|PubMed:29880641}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; MG852025; AYN71345.1; -; mRNA.
DR PDB; 6BFI; X-ray; 2.30 A; A/B=1-846.
DR PDBsum; 6BFI; -.
DR AlphaFoldDB; A0A3B6UES5; -.
DR SMR; A0A3B6UES5; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR46180; PTHR46180; 2.
DR Pfam; PF01044; Vinculin; 2.
DR SUPFAM; SSF47220; SSF47220; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton.
FT CHAIN 1..846
FT /note="Vinculin"
FT /id="PRO_0000451758"
FT REGION 1..257
FT /note="Interaction with TLN"
FT /evidence="ECO:0000269|PubMed:29880641"
FT REGION 617..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..370
FT /evidence="ECO:0000255"
FT HELIX 8..32
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 41..59
FT /evidence="ECO:0007829|PDB:6BFI"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 68..97
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 102..145
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 154..178
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 185..215
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 224..249
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 289..306
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 312..338
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 344..375
FT /evidence="ECO:0007829|PDB:6BFI"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 399..427
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 432..449
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 466..493
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 496..519
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 524..550
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 555..569
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 572..584
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 589..615
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 649..659
FT /evidence="ECO:0007829|PDB:6BFI"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 669..682
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 690..710
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 718..745
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 750..760
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 763..778
FT /evidence="ECO:0007829|PDB:6BFI"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 786..817
FT /evidence="ECO:0007829|PDB:6BFI"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:6BFI"
FT HELIX 826..829
FT /evidence="ECO:0007829|PDB:6BFI"
SQ SEQUENCE 846 AA; 91655 MW; 83CC17291DBC317C CRC64;
MPVKFHTKTL ESVIDPVAQQ VGQLVLFHEQ AESGLLKEDL TPLVQGVGIA VTNLVQVAAS
MVETSNDEDF KAELPPSMQE VQQAAVFLSD AARLLKADQG SPEGKRKLLD GARGVINGMS
DLLMCADRSE VRKMVKVCRS VQEYLDVAKV IDVEADLATF LQNLTPGMTS MMKVVEQRHP
ELTNLAHAQM LKSELGTVRE QIPILISSIR VCCLVIVKDG SSGMKDAAFG RDYVIQKLFI
AIEEIIRVLQ LTTTFEEEEV GGAGAASAAS LAHMFHQAQD ALASGDISRS TLDAVRKCIS
EGRRVAALAA TDETRAKLLA AADELDQILK ELEELQAKGL GDSRQARALA HAAAVKLQEL
EQEIRKALAE RVATDFVNVG GPIKALEDAA LASPSDPNRQ ANFAQKAKEF EAHTARLADT
AELVASSGGC SDAVAAELRK EAAKLRDIST AVVPAARVVL ENPGNQAAKD YLRTVKEKWL
EAAESMGRSV DGVIDSLEFM KVSEARIQAD VKEAKRIALA EEDSMKLIAK ASSVARQANR
VIQVAKVEAD NSENPEFVAK LSSASESLAK SISPMVIEAK AVVTSPQNKD IQRKFCSSAD
KVVEGVAAVR SVIEDNWVPP RPPLPELEEE EEPPELPPPP EDPASLLPAE MQEAEEMLRA
PLPPKDQNPI HHAAASVFRE ADQWDEKGND LISLVKQMAR KMAMMSKYTR GESGEVRSKA
DLIRMAKEIA LNAQELLKLA RQIANACMDK RAKTNLLQLL DRIPTISTQL KILATVKATS
MGGGDARADA DATDMLVGNA ENLMRTVKDV IRASEAACIR LRPDSPIASI LWRKKGGQGR
RISVSY
