ID A0A3Q0RSP7_AMPCI Unreviewed; 1002 AA.
AC A0A3Q0RSP7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cingulin {ECO:0000256|ARBA:ARBA00044075};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000013711.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000013711.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC tight junction (TJ) paracellular permeability barrier.
CC {ECO:0000256|ARBA:ARBA00043864}.
CC -!- SIMILARITY: Belongs to the cingulin family.
CC {ECO:0000256|ARBA:ARBA00038467}.
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DR AlphaFoldDB; A0A3Q0RSP7; -.
DR STRING; 61819.ENSACIP00000013711; -.
DR Ensembl; ENSACIT00000014081.1; ENSACIP00000013711.1; ENSACIG00000010611.1.
DR GeneTree; ENSGT00940000154489; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR Gene3D; 1.10.287.1490; -; 1.
DR InterPro; IPR002928; Myosin_tail.
DR PANTHER; PTHR46349:SF4; CINGULIN; 1.
DR PANTHER; PTHR46349; CINGULIN-LIKE PROTEIN 1-RELATED; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054}.
FT DOMAIN 646..956
FT /note="Myosin tail"
FT /evidence="ECO:0000259|Pfam:PF01576"
FT REGION 73..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 114646 MW; CD38EEE231FDCF3B CRC64;
MTTPSSDRKT PVDYGVQIRF INDLYENGGV QPVTQPKTKS QTASKYGVAV RVQGIDGHPY
VVLKDGKKGD SYGVQIKTQY SPGHNSLPRK REKADPGIEG DHVGGGGGDE DFQLSRPPGD
GKSGSYGNLD AGIGVRGDGE QGWHVSDREG GTERNMWHGS YQSGLNRSLG SVRDSPEPPP
QQYDLDYNKR QTSVNRLINR FGGVNAGGQQ RGLSPPQQHP RAASPPTTAN PYTLPASSTH
SSLGRSQGTF KVPGHSANQW TSVEPPQRNL TEAQVRIQSF VTPDLLLDQG QSAELSSEEE
QAMQTVYNIL RQGYRLPLYL PVATFAHIDN SDPALKAELE RCLDESLQLQ EMLDRKEKEL
NETQSELTQL RMDRENAEKR VREMEDQLAE FQDELRRENS NKTDLVSCQA QLMEFCQLKK
KLEETLRQRE RELTALKGAL KEEVATHDRE IEALREQYSA DMEKLRSSME QVSQSHAGIE
AERLRVNASV RSLQQQLEDC RDESSHWMEQ FHSTRDELRT TNEVTQLKKK LSLTEEELDS
SKTQLNRAHL DMNSLQDAQQ EQKEANTRLK EKISRLELQS NATESSEAEL ALHTEVRGLR
SELDEAKRKA SRLSQEHREL GQHLEDSEKD KETLRQTISQ LEDTKRQQER ALEKLNKENE
SVNMSLREEA QALRVQLDEQ KERARKEMQE AQRHGNDAQS ELERSQINIR KLEEEISRQK
KELLLACEER DNHQLDKELL TNRLRHLEGE LEASKNSHSE KTREIRILED KLKRLELEVE
EERSSVDMLT ERVARSRDQI DQLRSELMQE RSSKQDLELD KNAMERHLKE LRSRVADMEG
QSRSSAGVSQ LENKIQELEE RLRSEEREKN AVLATQRRLE RKLKDLNMTL DEERQTHTEQ
RDQLALRVKA LKRQVDEGET ELERLDGLRR KAQRDLEEQM ELKEALQARV TALETELKRK
TQAAMRPTLD SSALSSDDDD SLYDPSTITS ILTESNLQTS SC
//