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Database: UniProt
Entry: A0A452GPY3_9SAUR
LinkDB: A0A452GPY3_9SAUR
Original site: A0A452GPY3_9SAUR 
ID   A0A452GPY3_9SAUR        Unreviewed;      1713 AA.
AC   A0A452GPY3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000003891.1};
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:ENSGAGP00000003891.1, 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:ENSGAGP00000003891.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the RIMBP family.
CC       {ECO:0000256|ARBA:ARBA00010749}.
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DR   Ensembl; ENSGAGT00000004517.1; ENSGAGP00000003891.1; ENSGAGG00000003174.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd12014; SH3_RIM-BP_1; 1.
DR   CDD; cd12012; SH3_RIM-BP_2; 1.
DR   CDD; cd12013; SH3_RIM-BP_3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035753; RIM-BP_SH3_2.
DR   InterPro; IPR035755; RIM-BP_SH3_3.
DR   InterPro; IPR040325; RIMBP1/2/3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR14234; RIM BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR14234:SF18; RIMS-BINDING PROTEIN 2; 1.
DR   Pfam; PF07653; SH3_2; 2.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF50044; SH3-domain; 3.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50002; SH3; 3.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          446..513
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          768..863
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1433..1501
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1559..1626
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1300..1351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1360..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1535..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1646..1713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          185..212
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          237..334
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..437
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..950
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1039
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1537..1551
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1658..1681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1697..1713
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1713 AA;  192393 MW;  AAA02C63F5437189 CRC64;
     MKPPNRRPEA RTSEKTSASM SVQKTKDRSP SASSSSSTTS RTTTKTFPLK HKTHSVNMKS
     LQPPNTNHPS HGIKDLEIRL LQVECEELKN RLGCLREGLM GRKPSDMEEL LKQSQKELLW
     LQRQLSFIAT GGPTCILSAS QFRNDLPYLQ PAVPQKTLDR IRFVEEKTQI FQSNVTTLTQ
     ENHHWRFLEN ELKDAVQEKN RLSLQYASLS HKALQYDQVK SDYVQLRETL TIVTKERDLA
     VKEKHQLQAK LENLEQVLKH MREAAERRQQ LELEHEQALA VLNAKQQEIE LLQKAQVEAK
     KEHEGAVQLL EAKVRELEEK CRTQSEQFNL LSKELEKFRQ QAGKIDLLSS NSVASSDVLG
     SPSKSLSQLM NGIATSIGKG NESPSGSRCV ISEFIRPLQI SGDKPEQLSV KPTFLSRSRS
     SSPRCRFDSD MDNERNSNTS KQRYSGKVHL CIARYSYNPF DGPNENPEAE LPLTAGKYLY
     VYGDMDEDGF YEGELLDGQR GLVPSNFVDF VQDNESRLSS TVGSEQDQNF INHSGHALEG
     DSLLELNPPS HIESNVINNG TGTLDMNIDE IGEDIVPYPR KITLIKQLAK SVIVGWEPPV
     VPPGWGTINS YNVLVDKEIR MNVSFGSRTK ALIEKLNIAT CTYRISIQSI TSRGNSDELL
     CTLLVGKDVI VAPSHLKVDN ITQISAELSW LPTNSNYSHV IFLNEEEFDI VKSASYKYQF
     FNLKPNMAYK VKVMAKPHQM PWQLPLEQRE KKEAFVEFST LPAGPPAPPQ DITIQAGSTP
     ATIQVSWKPP TLTSTGTSNG ANVTGYGVYA KGQRVAEVIF PTAENTFVEL MRIRNVEAKE
     VTVRTLSAQG ESVDSCVAAI PPDLLVPPIT HPRTAPKSKP LASAGAPDTK DEHLGPRSKM
     DESWEQTRSA SPIHGHTLEP PAPNFQSPLQ GRRSPSPNRI LPQPQGTPVP NTVAKAMARE
     AAQRVAENNR MERRSVFSER SNMAHYANSD EEEDGYDSPS VKRRGASVDD FLKGSELGKQ
     PHYCQDEEYH TESSRGSDLS DIMEEDEEEL YSEMQLEDGG RRRVSVTSHN TLKECSKNRT
     TEAAFLEQPD FSQQTHHSKK LFSIPEVAEE DVEYSELLHK QGFGTSYKMK PMVARCTRPP
     RPYNQDKQHN FWYPAKHRIS GMEDFASEDK GYNYSKSLTR SPDSGLDCGS EEEESRFNFR
     NAYNLISANV APSYCAETDN CSCRKSTRPL LARRKTLTRQ SSIEEDFDDL GPSFIEPRSE
     EAKCGYEKKP ETQKCNRTDN LTGKDVQQVW KINLQVNDSR AAVPHAEPSH RDAEDSLLLG
     NPSSTGRPDR VEHTGRRLSH ASAVPQKSRP MLVPSIEITM DSNSEGGRSR SGSEGNISPV
     KEEAYYRRID GHKKWSQQRT MASDYRYDGY CSRDHLSPDI YEESETDPGT DDISPRIFVA
     LFDYDPLTMS PNPDAAEEEL PFKEGQIIKV YGDKDADGFY RGETCTRLGL IPCNMVSEIQ
     ADDEEMMDQL LKQGFLPLNT PVEKIVNCDR FKESTRSVHR RSRKSKRERN RRSGRQQSVS
     TRRMVALYDY DPRESSPNVD VEAELTFCTG DIITVFGEID EDGFYYGELN GQKGLVPSNF
     LEEVPDDVEV YLSDVPSRHV QDTPLRTKAK RVPPENTGTS RRAPSPTVHL HSGSPTPSMG
     SGSPGRGREM SSKKKKGLLS KGKKLLKKLG AVK
//
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