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Database: UniProt
Entry: W5NAV4_LEPOC
LinkDB: W5NAV4_LEPOC
Original site: W5NAV4_LEPOC 
ID   W5NAV4_LEPOC            Unreviewed;      1160 AA.
AC   W5NAV4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Integrin alpha-X-like {ECO:0000313|Ensembl:ENSLOCP00000017763.1};
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:ENSLOCP00000017763.1, 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:ENSLOCP00000017763.1}
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; AHAT01038658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01038659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NAV4; -.
DR   STRING; 7918.ENSLOCP00000017763; -.
DR   Ensembl; ENSLOCT00000017795.1; ENSLOCP00000017763.1; ENSLOCG00000014415.1.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000154838; -.
DR   InParanoid; W5NAV4; -.
DR   OMA; ACGPTWE; -.
DR   Proteomes; UP000018468; Linkage group LG2.
DR   Bgee; ENSLOCG00000014415; Expressed in camera-type eye and 12 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; 1.
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; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 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; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR048633; ITGAX-like_Ig_3.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF84; INTEGRIN ALPHA-L; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF21520; ITGAX-like_Ig_3; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00191; Int_alpha; 5.
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..25
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           26..1160
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5001426643"
FT   TRANSMEM        1102..1125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   DOMAIN          156..328
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          445..505
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          507..565
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          569..632
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ   SEQUENCE   1160 AA;  125617 MW;  219FEAF8FFC5A90A CRC64;
     MTSPRIKRSL WTLAVPLFYT HLCCCFNLDS QQPLVFHGEA AAHFGHRVCQ FGQAGNESVV
     VSAPLQANRT GHVYSCRFGT GQCERISLPG TGDAGIAMGL TLACDNKQLA VCGPQLQHDC
     DPIPYLNGFC VLLGPGFAVK ETLRPAFQEC RDSGLDAVIL FDDSQSISDT DFQTMIQFIK
     DVLRNFTDPK SQVAVAQYST NIRTVFSFNT FVSNRNPNSL LRNVPHTQGQ THTPSAIKYV
     LDNVFTKEQG MRQESKKLLV VITDGKSNDP KEKFENVIPL AESRGIIRYA IGVGKQISKQ
     ELKTIASSPK DVFEVNSFEA LNSILKQLGE KIFAIEGTNK KSNFTSFQLE LSQGGFSAAV
     TEESILFGAV GSFDWSGGFV EIRGGDLHGT FINASSREPE FADSYLGYAL AVAQLAEGRV
     YFAGAPRHTH RGTVLGFKKG RSAWEVAWRL NGTQLGSYFG AELCVLDVTG DGRTDLLLIG
     APLFHEPGTG GEVTVCTIAS EGFPNCSSSL RGSPGNEHGR FGTAIAATPD LDGDGIPDLA
     VGAPHEDERG GSLYIFLGHR RGVHTQHSQK VQGASVRSGL QFFGQSVHSA GDLSWDGLAD
     VAVGARGAAV VLSLPRSQPV INVSVAMTFT PNAITENNFH CARPIMSSTQ PATIATVCIA
     ITAVHAGKLS SGLSARVNVS VRLEPQAKTS RLLFVPGDPT THWTGTVNDS ACYNISIIVP
     ACISDYSPVP LSGNFTVEGE RMKVTDGLRP ILTPRCLTTF ADQVLLEQVC GEDQVCVSDL
     GVTINFTSLS PMVIASPRYT VIVQVAITNL GEDAYGTEMA LIYHSALSFT KASVTQSTWR
     SSLSCSGDDR QVNSTVVRRA SCQVSASVLK ERAKVTLHAF FTVSHPELLE DHLQLNVSVQ
     SKNENLTLED NFDSSTVPVL LPVDIVVEES CVSSADSTYN IIFLETSQTS SNMEHSYKVK
     NVGDVDLPVD MTFIVPVELR SGFVWNVSAP AEPIRQSMPC SLKQPYSWSP LTACSLPQFC
     NGTLCLHFGC KIDRLTRNQE VTFTFLGNII RNPESQKNGV QVTAESWSFL SFDERKYIQF
     PSSSVNRFSV NTVLEVPRQD SLVGIIVGSV IGGLVILIII SLAMAKMGFF KKFLQFVEKM
     KAGNGLLVPN GKSSEERAAQ
//
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