ID A0A452IPI9_9SAUR Unreviewed; 1228 AA.
AC A0A452IPI9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000029849.1};
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:ENSGAGP00000029849.1, 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:ENSGAGP00000029849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000256|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000256|PROSITE-
CC ProRule:PRU00841}.
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DR Ensembl; ENSGAGT00000033892.1; ENSGAGP00000029849.1; ENSGAGG00000021541.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR Gene3D; 3.10.20.360; CKK domain; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595:SF2; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 3; 1.
DR PANTHER; PTHR21595; UNCHARACTERIZED; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50346; PRC-barrel domain; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1228
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019022003"
FT DOMAIN 75..189
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1089..1223
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 133588 MW; A8E3064042B69D88 CRC64;
MGAHLAVIDS LMIAFAVEST HSLSAPPGTD LGAGSWEQKL LCWVDTVNRK LQESTEREGS
QQLVPGTEGQ SQSQSPASGP KIRYRKDKVL PKQTPCFTPV MGMKDLANGG AIAATIHYYC
PDVVRLEDVC LKETMSVADS LYNLQLIQEF CIKYLGGCCP LALEDLLYVP PVLKINIGVF
LAELFLCFEV LKPDFVRPKE LRGLKDPPAV SDSLTPSSGN SNSGSLVFSF LHPLLPGGQP
QSPLRGSLGS MHHSTSMSHV EGGFGKSWSK KQLSHPLSQA VSFSIPFGLD SDVDIVMGNP
VGMLRSISSD SLAPVPTRLA RSPGPLPEDA AQRLAKDEAP NGPVAPHRTV HKVALSAKGV
VEREGPPVEN GLADGYPDLP TIEEALQIIH SSERLHPEGA ADGFYLHSPE PAKPTQAPEP
TPALAVYRFH SGPPNGRAEA PTPPGNGSLD SDAEDPARLP GTKDDTSSGL SSLSSQPDSA
GSSGAGVRMT SFAERKKKLA PPEGKTLQKS TGESSEAGAV PPEDSPGRSP ALSSEMSQLG
ARLEEKRRAI EAQKKRIEAI FAKHRQRLGK SAFLQLKRRD GGEEEEEEEG EAKLSLEERL
ARLEAEEGGS LQVQAEEEGP GQGCPEKQVT FSSEIKGAPL DENLGDYNRA VAKLNTALSS
LQLDMHRLSQ QQQRLLQEKK PSQAWVIPAP KGPAPRASRE FVPPRSVELS SSPSPSPSRX
XXXXXXXXXP AAPRSPQPAP KKAAPTPPKS PKHARPVELK LPPLTRVLTP PHNVDTLPHL
RKFSPSQVPM QTRSSIHFSE EVAGPEQPLE SPELETQGNL RPVASVVPQG GVGSARVSGD
GTSDVSSPGE RRSSLIEIPL SSLQAEEGDG DDSLEESLTE VMDMEPRAGL GFFFKDDEKP
EDEMAQKRAS LLERQQRRNE EARQRKQWLE AEKEQKEEAA RLQAEERPRP EEEASPRRGD
FTRQEYQRRH QLKLMEDLDK VLRQKPTTVR ALKKGRPKTV FCDDSALARS PVKGLLGSRL
SKVYSQSTLS LSTVANEPGN SLTIKRPSRA ASPSGLMSPS RLLGSQSRER DWENASTASS
PASVPEYTGP KLYKEPSAKS NKHIIHNALS HCCLAGRVNE PHKNKILEEM EKSKAHHFLI
LFRDSSCQFR ALYTPAGETE ELTRLTGYGP RTISQAMIEG IYKYNSDRKR FTQIPAKTMS
MNVDAITIQG HLWQTKKPGT PKKPGTPK
//
