ID W5M6Q5_LEPOC Unreviewed; 1130 AA.
AC W5M6Q5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Integrin subunit alpha E {ECO:0000313|Ensembl:ENSLOCP00000004063.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004063.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000004063.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR EMBL; AHAT01005677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01005678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01005679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015222947.1; XM_015367461.1.
DR AlphaFoldDB; W5M6Q5; -.
DR STRING; 7918.ENSLOCP00000004063; -.
DR Ensembl; ENSLOCT00000004071.1; ENSLOCP00000004063.1; ENSLOCG00000003409.1.
DR GeneID; 107079925; -.
DR KEGG; loc:107079925; -.
DR CTD; 3682; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000161532; -.
DR HOGENOM; CLU_004111_3_2_1; -.
DR InParanoid; W5M6Q5; -.
DR OMA; YIFNGFK; -.
DR OrthoDB; 3816176at2759; -.
DR Proteomes; UP000018468; Linkage group LG22.
DR Bgee; ENSLOCG00000003409; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF79; INTEGRIN ALPHA-E; 1.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF20805; Integrin_A_Ig_2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00191; Int_alpha; 4.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 3.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 18..1130
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5001426606"
FT TRANSMEM 1086..1108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 188..368
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 478..538
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 539..598
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 602..662
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 148..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 125426 MW; A95E3A7B7112F7B2 CRC64;
MAHNCLLWLI TVYAVEGFNI YSKPIKTFEE LNSPSLGQSV LQYEDGILVT SPLDNMSDQQ
YGRLYDCKVS AQCTEVSLTA KEKSYRKPII SAAKSSDGST YLVCQQHRTR KATNEDLNGV
CSLLKAGFQE ISDIAPASLV VKQMKRNNTN ANKQEDESLS VNSGSALHRR KRESSNQEEE
EDEDAGTEIA FVLDGSGSIS GEDFERAKEF VTNVMKNVWE TCFDCRFALV QYGKDIRTEL
SLKENEKPEY ALRKVSDIQQ IYNYTKTASA MYHVLEHVFV AENGSKENAK KIMIVLTDGK
IFLDTMNLSD VLMMPKMKAV TRFAIGVGAD FNQTKAVTEL QDIASDPDDE HLFKVDNYAA
LDGILSLLEK SITGIEGTQQ GAAFLFELSE AGFSIDFAID GTVLFGAVGA YDWNGGLIIK
NPDDTIRFLN ESSTKEKLSY LGYSVAAVKG VSGSLYVSGA PRHSFSGSVL VFNGTSHAAQ
QTLSGEQVGS YFGAELCVLD TDKNGITDHL LIGAPLFHQK GEEGKVYVYR LSQGLFIKES
EWRGMNRYTF ARFGSAIANI GDIDDNGYND IAVGAPMEGD GKSGSIYIYN GYENGIKDHH
SQRIAAADFD VKLRFFGQSV SGMSDLDKDG QIDISVGSLG KVTVLSSLPV IVFKPQVTLD
PPYISLNKQS GQDSKKISAK ICFNSVKREI KKKTEELPIH YHLVLDPNKE KKRLSFANGD
PKSISGIFKL TNTMECLPDI LLQFLECADD CFSPVEIKLN FTLNLSSESR PLRVLDMLSP
NEISQQLPFE TNCGTDKICT ANITLSTSLP QDKTLVIGST KDLSLGFNMK NIGEDSHMTI
LVLTYPHFLQ YNKLSLLTEN KGISCANPVD NTKLTCQIRY PVMKAQSEVN FTISWQIEES
HKIQENSTQI TANITCENNG LQVLTEETYR FAVKNALKVS LTGKAKPAYI HVTEESMGKK
QELEYLFQIH GENRYNANIV VNIDIPLKER DTQVTIVSYK ARHTTNCSAQ PQDNGKTYRL
TCTVQELDEL LTVEASVAVI SIKDQRENLT ARAFLSFDSA QYEADEGGRY EEVLVTIEKL
TVVKSMAVIV GSSIGGFVFL AFLILILIKC GFFRRRYQKA RVEQKSDQDM
//
