ID A0A3B4VGT9_SERDU Unreviewed; 1125 AA.
AC A0A3B4VGT9;
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 alpha-11-like {ECO:0000313|Ensembl:ENSSDUP00000029782.1};
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:ENSSDUP00000029782.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000029782.1}
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; A0A3B4VGT9; -.
DR STRING; 41447.ENSSDUP00000029782; -.
DR Ensembl; ENSSDUT00000030294.1; ENSSDUP00000029782.1; ENSSDUG00000021465.1.
DR GeneTree; ENSGT00940000155465; -.
DR OMA; AQHSQRK; -.
DR Proteomes; UP000261420; Unplaced.
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; 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; 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; 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; 4.
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT TRANSMEM 1086..1112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 40..98
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 180..361
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 482..543
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 546..604
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 608..668
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1125 AA; 124733 MW; 9D99C030CB35DAA7 CRC64;
MNGLDWLYWA AFSSQSNQLS VEITIFFCVT DLQLCFNFDT KNFKIFSGSK ETQFGYTVQQ
HEAGGRQWLL VGAPFESTGK QQTGDVYRCP LDTRASANCS RLHLGKLSLD NVSERKDKMR
LGMSLTSNPR DNSFVTCGPL WSHECGSSLY STGICSRVSR NFRLSHTIAP ALQRCETFMD
IVIVLDGSNS IYPWYEVQDF LINILQKFYI GPGQTQVGVV QYGSTVVHEF SLGEYQTVEE
VVEAARSIDQ RGGEETRTAL GINVARSEAF KRGGRPGAQK VMIVITDGES HDSPQLVQAV
GDSERDNITM YAIAVLGYYN RRGINPEAFL KEIKFIASDP DEKHFFNVTD ESALKDIVDA
LGERIFTLEG TSSQGRGFGL QMAQAGFSSH LVKDGVLLGA VGAYDWNGAV LKETKHGKIV
PPKSSYKDEF PEELKNHGAY LGYSVGSLIS SRGSQLYVAG APRFNHTGKV IVFTLKNNGN
LTILQALLGE QIGSYFGSEL LSMDVDGDGQ TDILLVAAPM YYSQGWERGK VYIYSVTSQV
NTHFLQGALQ ISDRSQNSRL GSALTQIPDM NGDGFRELVV GAPLEDDHQG AVYVFYGQDK
TIQHQYRQRI SAAGFSAGLK YFGQSLHGVL DVNADGLVDL TVGALGAAVI IWSRGVVRIQ
AKLTFEPEKV NIFNKDCWRG GKEVTCMSVS VCLSLDSRTK TRTKTRTAVW FSLVLDERRF
PPRAVLDESD RQQPRSLSLQ AGGQSCQRLG FSVQETTDYG RPITVVLETG MQNPDEGPVL
DPDWPSIMRA ELPFWNGCEQ EDVCVPDLVL HSRTDLMDVQ QFCSSRDRAT WSLCGQQGAS
LRSAFVVESG RRRLVMFSQL VNEGENAYGA AIHISTSSNL IFSSLIVKDQ SDIQIECSSE
DRLATQRFCN ISAPFMKSLS QVVSTVFSPV CVCVLTSEGE DGFPDDNLSD ILLPLKYQTD
LLFTRHSFLI LFSFCSFTLD MQIQNLGIFS VHDLLFRADI WALTAKGNQL VNITDYSIEQ
VTQEMNEPFR GPYVHSVSVS LFQVSFRSLE LLTAASIQLD ASSPMFLQED RPVRQIILEL
RKDEDYIVPV WIILGSSLGG LLLLALLVLA LWKVTTHNSK TTNLL
//
