ID A0A8C1QH42_CYPCA Unreviewed; 2308 AA.
AC A0A8C1QH42;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCCRP00010039491.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010039491.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010039491.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSCCRT00010043378.1; ENSCCRP00010039491.1; ENSCCRG00010016802.1.
DR Proteomes; UP000694427; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:TreeGrafter.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 5.
DR FunFam; 1.20.900.10:FF:000001; Guanine nucleotide exchange factor DBS; 1.
DR FunFam; 2.30.29.30:FF:000091; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000038; kalirin isoform X1; 1.
DR FunFam; 1.20.58.60:FF:000034; kalirin isoform X2; 1.
DR FunFam; 3.40.525.10:FF:000003; kalirin isoform X2; 1.
DR FunFam; 1.20.58.60:FF:000023; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.58.60:FF:000032; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.900.10:FF:000008; rho guanine nucleotide exchange factor 25; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH_dom.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR058918; KALRN/TRIO-like_spectrin.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR051336; RhoGEF_Guanine_NuclExch_SF.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR055251; SOS1_NGEF_PH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF106; TRIO, ISOFORM A; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF23587; SH3_KALRN; 1.
DR Pfam; PF22697; SOS1_NGEF_PH; 2.
DR Pfam; PF00435; Spectrin; 4.
DR Pfam; PF23323; Spectrin_6; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 5.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694427};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1794..1816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..186
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1264..1438
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1574..1639
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1811..1969
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1981..2091
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2158..2223
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1755..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1722
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2114..2132
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2308 AA; 263303 MW; CD69DA9EF2C6FFDF CRC64;
MNSAEAAEEG PNDPDTEPFF KTVPSFSSGS LRNDGINAAD VLTVLREKVA FVSGGRDKRG
GPILTFPARS NHDRIKQEDL RKLVTYLSTV PSEDVSKRGF TVIVDMRGSK WDLIKPLLKT
LQESFPAEIC VALIIKPDNF WQKQKTNFGS AKFTFETSMV SVEGLTKLVD PSQLTADLEG
TLEYNHVEWT ELRVSLEEFT GGALHLLSRL EELQEVLSHQ ELATNAEEAR KLLEEHARLR
KTMTKAPVDE LDHEGQRLLQ KIRDGGDGRL SGGADFQSLV PKISALLDKL QVTRQHLLQA
WHNRKQQLDQ CFQLRLYEQD AEKMFEWIGH NKELFLQTHT DIGVSNQHAA DLQTQHDHFA
MNSMNAYVNI SRIVSVATRL CEAGHYAAAQ IQQISGQLDQ DWKSFASALE ERSAILAMSS
VFHQKSEQFL SSMEGWVKSC GEGGLPTAAQ ELEIAIHNHQ NLYEQVTTAY TEVSQKGKTL
LDVLQRPQPL PDSGSLTAGA DYSQAVRGVL EVVHEVVHQY RRLEGLLQHR KLRLHQRLQL
CVFQQDVQQV VDWIENHGEA FLSKHTGVGK SVHRARALQK RHDDFQEVAQ NTYTNADKLL
EAAEQLAQTG ECDPEEIYAA AHHLEVRVQE FVRRVEQRKL LLDISVSFHT HTKELWSWME
DLQKTLVEPV VNSESVDAVQ ELIRQFQQQQ SSTLDATLNV IKEGEELIQH LRDSALACNK
LPHASSVAHI EGVLQQLDEA QAHMEEVFHE RRIKLDIILQ LRIFEQYALE VMGELDAWKQ
DLMRQASDFN TEELTLAEQR LHRHTERKLA MNNMTYEVIQ QGQDLHQYIM EVQASGMEIT
GEKDVDLAAK VQELLEFLNE KQHELEVSAE HTHKRLEQCL QLRHLQAEVK QVLGWIRNGE
SMLTASTTNA GSLSEAEQLQ REHEQFQLAI ERTHQSALQL QQRAELMLQA GHYDPDAVRA
CAETVALHWQ TLMLKMEDRL KLVNASVAFY KTSEQVCNVL ESLELEYRRE EDWCGGHDKL
GSTADTDHVS PLINKHLEQK EAFLKACTLA RRNAEVFLKY IHRNNVSMPG VATHNRATES
QVKAILSELL QRENRVLHFW TMKKRRLDQC QQYVLFERHA KQAIDWLQET GEYFLSTHTS
PGDTSEKTQE LLKEYDDFRV SAKQTQEKVK LLIQLAGSLV EKGHLHVTEL RRWVSTVDRR
YRDFSMRMGQ YRCSLDRAIG VCSEDNKDLE LDIIPASLTH TDPEVNLNDP DHEVNEEKKK
SARKKEYIMA ELLQTERAYV RDLQECLETF LWEMTSGAEI PSGIANKEHV IFGNIQEIYE
FHNNVFLKEL ENYEQLPEDV GHCFVTWADK FHMYVTYCKN KPDSSQLIQG QAGRFFDEIQ
RRHGLANSIS SYLIKPVQRI TKYQLLLKEL LTCCEEGKGE IKEGLEVMLS VPKRANDAMH
VSMLEGFDEN LAVQGELILQ DTFQVWDPKS LIRKGRDRHL FLFEISLVFS KEMKDSSGRT
KYVYKNKLLT SDLGVTEHIE GDPCKFALWG GRTPTSDNKT VLKVRCVDVY VCVYQCQINL
QIWQSRIIVA SLSGGCEQTV VLQDFVAGSV GELSIQSGQT VELLERSGER PGWCLVRTTE
HSPPQEGLVP SSTLSVSHSR SSVDMDCFFP PGKEVKSESA ASLQPQTSVT SLPTSSPGPK
RSGTTGNTLK KWLTSPVRRL SHGKGDNTNA KKPNNKQRKR DGRKSVELGP PHQDSIDEVQ
QLTIKYLENM LRGRRGVNSG GEEEAEDEPH TPLPPPMEII KDPSTQEEKV KHRLYFIFIV
VLLFSFFDST SLILFVKGGF MRRIGEKGVP EEMTGKDKIV FGNIHQIYDW HKEFFLCEIE
KCLQDQDRLA ELFIKHERRL HMYVIYCQNK PRSEFVVAEY DAFFEEVQQE VNSRLSISDY
LIKPIQRITK YQLLLKVLAT ELHNDYTLTI LSMKAVDLMS LVPKQCNDMM NLGRLQGYEG
KLTAQGKLLQ QDTFFVTEQD SGVLSRSKER RVFLFEQIVI FSELLRKGSS TPGYQFKKSI
KVSYLSMEEH VDSDPCKFVL SCRGSSERLT LQAANIDIKK EWVQSIRELL DMQINFLTAL
QNPQEYQKKE SGGTLSRQLS NSSRSSSSHP STPLKPNTAP NGNVSFLCFQ ELDEEECNGL
SLVLVTQDYN AVKEDEICVV VGEKVQILAS NQQNMCLVYR PANSQSPAAE GWVPGHVLSS
TRFKCIILYH FKYVHNIFDI AIIDTQQRKM FPLFLSGSRK KKTQLNPGSP HCLQNPTLCF
FLHSTSDLVC NKLSSQSYQN RCLLKSVD
//
