ID A0A3B4T231_SERDU Unreviewed; 1203 AA.
AC A0A3B4T231;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Integrin subunit alpha 11 {ECO:0000313|Ensembl:ENSSDUP00000000062.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000000062.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000000062.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4T231; -.
DR STRING; 41447.ENSSDUP00000000062; -.
DR Ensembl; ENSSDUT00000000095.1; ENSSDUP00000000062.1; ENSSDUG00000000114.1.
DR GeneTree; ENSGT00940000155465; -.
DR OMA; HGIGPPF; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd01469; vWA_integrins_alpha_subunit; 1.
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; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR048286; Integrin_alpha_Ig-like_3.
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:SF21; INTEGRIN ALPHA-11; 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; PF20806; Integrin_A_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; 3.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 5.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
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 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..33
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 34..1203
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5017099947"
FT TRANSMEM 1156..1177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 35..97
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 179..360
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 370..421
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 481..542
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 544..602
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 606..666
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1203 AA; 134700 MW; 87D5DBD8D97E889C CRC64;
MHMHMHACTG KHMEYYCFLL LWICSQQLGV LDCFNIDTKK HRIIKGPKQA QFGYTVQQHV
AAGGEKWLLV GAPYEMNGPY QTGDIYKCSL SKRTNGGCSK LNLGRISLTN VSERKDKMRL
GMTLTSNPKD NSFVACGPLW SYECGSSYYS TGICSRVNAS FKFSRTIAPA FQRCETYMDI
VIVLDGSNSI YPWYEVQAFL INILQKFYIG PGQIQVGVVQ YGEKVVHEFK LSDYKSVEEV
VKRARSINQR GGEETNTALG INVARSQAFK QGGRRGAKKV MIVITDGESH DSPDLQQAIE
DSEKDGITRY AIAVLGYYNR RGINPEAFLN EIKYIASDPD DKHFFNVTDE SALKDIVDAL
GERIFSLEGT SKNGTAFGLQ MSQAGFSAHN VEDGILVGAV GAYDWNGAVL KETRQGKVVP
PKSSYTQEFP EELKNHGAYL GYTVTSVVSA KNGRLLVAGA PRFNHTGKVI IFTLKNSGNL
TILHSLKGQQ IGSYYGSEIA PLDIDGDGIT DNLLVSAPMF FSAGMEKGKV YIYRVTELNR
FILEGALEIH NGGQNARFGS SLAPVPDLNG DGFNDLVVGA PLEDDHKGAI YVFFSQHNRI
IRKYKQRIAA ADLAPGLQYF GRSIHGTMDM NDDGLVDLAV GSLGAAVLLW SQSVIRIYAT
VRFEPSKINI FVKDCQRGGK DVTCMSAIVC FNITARTAIL PTQEIGIKYN VSIAERRFNP
RAILDNPNKL QPQNLTLLPG EETCEHIYFH VMETTDYARP IVFAVQVGLQ DPDQGPVLDE
SWPTVVRTEL PFWNGCDEDD RCIPDLALQS MTDLMTRNQF CAQHVQSRGA FCRHISEQGL
EGSLRVLEGN RRRMVVDVRL ENKGENAYHT RLNITYTHNL RFSSLIVKDN SDIKIECYNE
DKLRNEKICN VSAPFMRAKS QVTFRLEFEF SRTVFLDHIR VILEAGSDGE EMSTADNFND
IYYSLKYEAD ILFTRDSNPT RYEIKSELSL EEPGVIGPPV NFTFQIQNLG YFPVKDLQLN
IEIPEMTKNG NQLLQISDFH IDQRDGTHCL PPQHVAQSRA SPEDLSRVSR LNQSNTLTLP
IQCAVNVASH REIAVRITGA LRIDTLHALK FKILELVTSA SVELPSSSPM FLHEARPVRH
ILLEIRKEGD YRIPTWIIIG STLGGLLLLA LLSLALWKLG FFRRQKRRDE DEREANGKVA
EER
//
