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Database: UniProt
Entry: A0A452IVP3_9SAUR
LinkDB: A0A452IVP3_9SAUR
Original site: A0A452IVP3_9SAUR 
ID   A0A452IVP3_9SAUR        Unreviewed;      2457 AA.
AC   A0A452IVP3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000032150.1};
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:ENSGAGP00000032150.1, 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:ENSGAGP00000032150.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826}.
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DR   Ensembl; ENSGAGT00000036449.1; ENSGAGP00000032150.1; ENSGAGG00000021400.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR   CDD; cd00176; SPEC; 12.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.58.60; -; 20.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR035825; Alpha_Spectrin_SH3.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF422; PH_9 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 20.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 20.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 18.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          967..1026
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          2308..2343
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          2351..2386
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   COILED          290..324
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          386..416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          858..889
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1126..1160
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1681..1715
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2160..2192
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2457 AA;  283412 MW;  C74835D4EA6E00B6 CRC64;
     MDPCGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDADELEKWI
     QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAII KLDETGNQMI NEGHFASETI
     RTRLQELHRL WELLLEKMRE KGIKLLQAQK LVQYLRECED VLDWINDKEA IVTSEELGQD
     LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ FAGKLIQEQH PEEELIKSKQ DEVNAGWQRL
     KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
     ERDLAALEDK VKALCAEADR LQQSHPHNAS QIQVKREELI ANWEHIRTLA AERHARLNDS
     YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA
     DESGQALLAA GHYASDEVRE KLTILSDERT ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
     NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
     KEDVATRRDA LLSRRNALHE RAMYRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
     YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYASDEVA ARMNEVISLW
     KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH
     ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DADNIKKKQE ALVARYEALK DPMVARKQKL
     ADSLRLQQLF RDIEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
     KAVTQKGNAM VEEGHFAAED VKAKLNELNQ KWESLKAKAS QRRQDLEDSL QAQQYFADAN
     EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLT AYGSSMQALR EQAQSCRQQV
     APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
     VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTLITKEVS SVSLRMKQVE ELYHSLLDLG
     EKRKDMLEKS CKKFMLFREA NELQQWINEK ESALTNEEVG ADLEQVEVLQ KKFDDFQKDL
     KANESRLKDI NKVANDLESE GLMAEEVQAV QQQVCDETDS KTTSPWKVGF ISIFPFQELN
     ERWRSLQQMA EERSQLLGSA HEVQRFHRDA DETKEWIEEK NQALNTDNYG HDLASVQALQ
     RKHEGFERDL AALGDKVNSL GETAERLIQS HPESAEDLQE KCTELNQAWN SLGKRADQRK
     EKLGDSHDLQ RFLSDFRDLM SWINGIRGLV SSDELAKDVT GAEALLERHQ EHRTEIDARA
     GTFQAFEQFG QQLLAHGHYA SPEIKEKLDI LDQERADLEK AWVQRRMMLD QCLELQLFHR
     DCEQAENWMA AREAFLNTED RGDSLDSVEA LIKKHEDFDK AINVQEEKIA ALQSFADQLI
     SADHYAKGVI SNRRNEVLDR WRRLKAQMIE KRSKLGESQT LQQFSRDVDE IEAWISEKLQ
     TASDESYKDP TNIQSKHQKH QAFEAELHAN ADRIRGVIDM GNSLIDRGAC AGSEDAVKAR
     LAALDDQWQF LVQKSAEKSQ KLKEANKQQN FNTGIKDFDF WLSEVEALLA SEDYGKDLAS
     VNNLLKKHQL LEADISAHED RLKDLNGQAD SLMTSSAFDT SQVKDKRDTI NGRFQRIKSM
     AAARRANLNE SHRLHQFFRD MDDEESWIKE KKLLVSSEDY GRDLTGVQNL RKKHKRLEAE
     LAAHEPAIQG VLDTGKKLSD DNTIGKEEIQ QRLAQFVDHW KELKQLAAAR GQRLEESLEY
     QQFVANVEEE EAWINEKMTL VASEDYGDTL AAIQGLLKKH EAFETDFTVH KDRVNDVCAN
     GEDLIKKNNH HEENITAKIK GLRGKVSDLE KAAAQRKAKL DENSAFLQFN WKADVVESWI
     GEKENSLKTD DYGRDLSSVQ TLLTKQETFD AGLQAFQQEG IANITALKDQ LLAAKHIQSK
     AIEVRHASLM KRWNQLLANS AARKKKLLEA QEHFRKVEDL FLTFAKKASA FNSWFENAEE
     DLTDPVRCNS LEEIKALREA HDAFRSSLSS AQADFNQLAE LDRQIKSFRV ASNPYTWFTM
     EALEETWRNL QKIIKERELE LQKEQRRQEE NDKLRQEFAQ HANAFHQWIQ ETRYSLSCMV
     EESGTLESQL EATKHKHQEI RAMRSQLKKI EDLGAAMEEA LILDNKYTEH STVGLAQQWD
     QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF DKDKSGRLNH QEFKSCLRSL
     GYDLPMVEEG EPDPEFEAIL DTVDPNRDGH VSLQEYMAFM ISRETENVKS SEEIESAFRA
     LSSEGKPYVT KEELYQNLTR EQADYCISHM KPYMDSKGRE LTSAYDYIEF TRSLFVN
//
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