ID A0A452GWY2_9SAUR Unreviewed; 1180 AA.
AC A0A452GWY2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000006542.1};
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:ENSGAGP00000006542.1, 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:ENSGAGP00000006542.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {ECO:0000256|ARBA:ARBA00038352}.
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DR AlphaFoldDB; A0A452GWY2; -.
DR Ensembl; ENSGAGT00000007613.1; ENSGAGP00000006542.1; ENSGAGG00000005303.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05894; Ig_C5_MyBP-C; 1.
DR CDD; cd05748; Ig_Titin_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR040849; MyBP-C_THB.
DR PANTHER; PTHR13817; TITIN; 1.
DR PANTHER; PTHR13817:SF164; ZORMIN, ISOFORM J; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 7.
DR Pfam; PF18362; THB; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 380..467
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 472..541
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 562..653
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 662..761
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 762..873
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 877..965
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 974..1069
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1087..1177
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 132831 MW; F4E757F250876FC1 CRC64;
MPEPTQQAEK ETKAEILPPA ETTPPAEQKK PKEDGTEQAK DMNVSESTSS SEDEDDSASV
NAPQADGTTQ SAERKDSVWS LGDGTPEETE KHDDSQRSTL FIEKPQGGSV NVGENITFIA
KVEAKDLLRK PTVKWFKGKW MDLASKAGKH LQLKETFERH SKVYTFEMQI IKAKENYGGN
YRCEVTYKDK FDSCSFDLEV HESSQPAPSI DIRSAFKRSG EGQDDAGELD FSGLLKRREI
KQEEEPEIDV WELLKNANPS EYEKIAFQYG ITDLRGMLKR LKRMRREEKK SAAFSKILDP
AYQVDKGGRV RFAVELADPT VELKWYKNGQ EIRPSTKYIF EHKGNERILF INNCTMADDA
RYHVTAGDEK CSTELFVREP PVVVTKALED LSTYVGERIE LSCEVSEEGA NVKWFKNGVE
LTNEPRSRYR LKVDGKKHTL IIEEATKADN ATYSVMTTGG QSAAKLAVDL RPLKIMQPLT
DQTVRLGKEI ALKCEISENI EGKWYKNGQL LPASDRVKLY HKGRIHRLVI ESSIVDDEGD
YMFVPDAYKI NIPCRVHVID PPRLHLENLG DNNTVTVLAG NKLRLEIPIS GEPTPKVMWS
KGDKWIMETG GRIRAETYPD SSCLVIDIAE RDDSGVYKIM LKNEAGEDSA NINIKVVDIP
DPPLAPNVTE VGEDWCFMNW EPPAYDGGSP ILGYFIERKK KQSSRWMRLN FDLCKETTFE
PKKMIEGVAY EVRVFAVNAV GISKPSMPSK AFVPLAVTSP PTLLAVDGVT DSTVTMKWRP
PDHIGAAGLD GYVIEYCFEG SISADLCDEL VEATYDLEAE EWIVANPELT DKTRYTITDL
PTGSRIFVRV KAVNAAGPSE PRLHPQPILV KEVIEPPKIR LPRHLKQTYI RRVGEAVNLV
IPFQGRPRPK VSWKKNGASV DKNQINIRNS ENDTIIFIRK AERSHSGKYD LKVKVDNLVD
KATIDIQVVD RPGPPHVVKI EDVWGENVAL SWQPPKDDGN AAITGYTIQK ADKKSMEWFT
VIEHYHRTSA TITELIIGNE YYFRIFAENM CGLSEDATMT RESAVIAKDG KVYKNPIYED
FNFTEAPMFT QPLINTYAVA GYNATLNCSV RGNPKPKITW MKNKVTIIND PRYRMFGNQG
VCTLEIRKPN PYDGGTYTCK AVNELGEAAV ECKLEVKVAQ
//