ID A0A3B4VNX9_SERDU Unreviewed; 1103 AA.
AC A0A3B4VNX9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Integrin alpha-M-like {ECO:0000313|Ensembl:ENSSDUP00000032244.1};
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:ENSSDUP00000032244.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000032244.1}
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; A0A3B4VNX9; -.
DR Ensembl; ENSSDUT00000032797.1; ENSSDUP00000032244.1; ENSSDUG00000023147.1.
DR GeneTree; ENSGT00940000154838; -.
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 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; 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; 2.
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..19
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 20..1103
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5017105848"
FT TRANSMEM 1051..1070
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 150..327
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 437..498
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 504..560
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1103 AA; 121573 MW; 25652CC797F1BE3E CRC64;
MDFIITATIF LTVLKTAPCF NIEPVAWKSW SNRAAGFGYQ VVQRQSDLLV SAPLQQYSPN
ERGEIYKCTT EGVSCQKLPI SVPAFAVNMS LGLTLTRDPT NQNTMACGPT IPKDCRSITM
YNGVCFAIDP SSRVGLPIPS SLEDCRAEAD IAFLLDGSGS VSGPDFRRMK EFVIDLVRTL
MGKGRQFAVA QFSSSHHIHY YFDNFFTSGQ WEYNINGIYQ QMGGTYTAKA IRYVVENIFT
PRKGSRPNVK RILIVITDGA SHDRGQLSNA AQSAEQKKIV RFAIGVGSAF SDVNAKNELI
TIASSPSSDH VFQVENFEAL QKIRQNLQDK IFSIEGSQSS GETLKMEMAQ AGFSVAFVPG
AIQMAVVGAN QWRGGFLRYT RTSQLPFEPV SMEPDSYLGY SMAVAITRRN SPLTVVGAPR
YKHVGIVMAV DKYQNQQVID PSPWQFQTGE YFGAEVCAMD MDLDGFTDLI LISAPMYKDS
DREGRVYVCM LRDLKVECRL DSPVILRGVA SDKGRFGSSL AALPDLNEDK LSDLAVGAPL
ENDGQGSIYI FLGERRSGIN DTYSQRIAAS EVQSGLKFFG MSISRWSSDQ SGDRLPDLAV
GSKGKVVLLR SKPIVMVVAT VSFNPNQIPT QQSSNDCKQP LNNSARICFT MTRESTVATA
QARINYTLTL DATRKAPNNR AYITENQQEK TGSIILVLNE QKCLTENFLI DACPEDALNV
LSNELKFTFD GLPSNTNLKP SLSQQAQTTT IHPLGFEINC GNDNNCVDNL KVDFNFTRSS
EVKVGIDELL NVTVTVENSG ENSYNSRVIL TYPAGLSYRK FTSLQGRIEC NSLDSEDGLS
RGRTDCTIDK PIFKSNTKAS FIVSYGIETN NQLQRRIFVT ANATSGNLEH SSSNELYKMR
EIDVKYSIFV TVESSLSYNN FTYGKNDLQK PVQQSLVVTN DIRALNFTVV IKVPVKLGDK
DIWVDSDSLQ IPNCQRDTDE QASVKDFVAQ IQKNKVVDCS VAKCRVFKCT RFMGRLESRK
YKISANLSSG WIEQIKAEVE VYPEPNFTKE IVGGSLGGLA LLALLTAGLY KAGFFKSKYQ
EMINDAGGEG AGADEGGATP DQA
//
