ID A0A452GHN3_9SAUR Unreviewed; 1136 AA.
AC A0A452GHN3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=VWFA domain-containing protein {ECO:0000259|PROSITE:PS50234};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000001129.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000001129.1}
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; A0A452GHN3; -.
DR STRING; 38772.ENSGAGP00000001129; -.
DR Ensembl; ENSGAGT00000001264.1; ENSGAGP00000001129.1; ENSGAGG00000000913.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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; 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:UP000291020};
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..28
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 29..1136
FT /note="VWFA domain-containing protein"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5018819912"
FT TRANSMEM 1097..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 157..331
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 445..507
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 508..566
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 570..630
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1136 AA; 124880 MW; 3633706037EE2E97 CRC64;
MARTPSAFPL LLLLLLRLPL QGPAPTLGYN IDTIHPKVLA PEASRTFGYQ VLQFRDGSII
VGAPGDQNST GQLYQCAVKK GSCQAIPLPA SAQMVHLGMS LASRDAEAQM IACGSGLSRT
CDANQYLSGV CYLFKGHLEQ PKELTPGFED CLKGNVDLVF LFDGSRSMNS DQFNAIKEFM
IEVMEKLGNS TIHFAAVQFS LAVKTEFDFN DYKRNRNPRE LLKNVKHMES LTHTFKAINY
VANQVFTPER GAREDVARVM IIITDGDPSD PGGNVNAAKE KNIVRYIIGI GNNFNWNRSQ
AFLTQMASEP TSQFVKVLDS FEKLKGLFSE LQAKIYAIEG TSSRSSFHLE LSSSGFSVDL
SKERVVLGAV GADDWAGGLI ELQSNQALET FIRSPIANEQ IKDAYLGYAV KSMQHQNRTL
YAAGAPRYQH VGMVIVFEID PGSSNWTDTQ HLMGKQIGSY FGSVLCSVDV DGDGDTDVLL
VGAPLYYEER SGGRVHIYRW DQAGLTSAAV LQGALGNPLG RFGAAITALA DLNGDGWADV
AVGAPLESEE HGAVYIYNGH QRELNTHYSQ RIEGTTISPG VKYFGQSIHG QIDLGGDGLP
DLSVGALGEV IMLRSQPILT VVPKMSFSPE EIPVKQVECS GSVSSRQGVQ SNLTICFSVS
RATMRYQEPL SANLTYWLEI DANRMRSRGV FGNRQRNMSG TMAISEGEPC IAEMIQISNC
IEDFVTAIKV SLHFALHEDN GSSRPPHLVL NPLHNSSMTE IPFEKNCGED GVCSANLQIR
FHQNTSQQLL VSPSTRLEVV LELINRGEDA YHTAVHLPQL PGLSFRKASV LESSVQARVS
CNGLETPDTN SRNLSCNVSH PIYWGNSRVL IQLLFDILTN SSWGDYLELD VMASSDNDMN
RTLVDNQDSH RIPVLYPINI ITKGADGSTQ YISFSSPNPE IKPVQHVYQV ENLLPGSFQQ
PEVTAFVMVP QKFLAGLAWE RQEVKTDPNV TCHPVAMNGK TKEADVNSVP SHTLKHCSPR
YQQIYKCNLG RIDAPSTITI IGALSVTSKI ETSSRSRFCT ALWFTFNTRK YLSQYTDEFT
QSQVTTEVEL VHVMNYLPVY IGSGVGGLLL LILISVVLYK VRWAGTGWAI GPWATQ
//
