Conserved Protein Domain Family

cd08682: C2_Rab11-FIP_classI 
C2 domain found in Rab11-family interacting proteins (FIP) class I
Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
PSSM-Id: 176064
View PSSM: cd08682
Aligned: 8 rows
Threshold Bit Score: 191.127
Threshold Setting Gi: 291225374
Created: 24-Mar-2010
Updated: 2-Oct-2020
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
Format: Row Display: Color Bits: Type Selection:
XP_002126079    7 VVVTVRQArnllvKGKSGSNEAYATIEFckdKYLTSTDKs--tTPRWFTQCSFTlpqggvfhnkivvhVTVMNKRHGKlg 84   Ciona intesti...
XP_421784      15 VQVTVLQAkglkpKGKSGTNDAYTIIQLgkeKYSTSVAEkt-lDPVWKEEASFElpgllmq-enpdryILYLIVMHRSlv 92   chicken
NP_001089307   14 VQVTVLEArelhpKGKHGTNDTYTIIQLgkeKYSTSVMEkt-lSPIWKEEASFElpglvme-enseqyQLQLTVMHRSlv 91   African clawe...
AAH57524       40 VQVTVLQArglrcKGKNGTNDAYAIMQVakeKFSTSVAEks-vAPVWKEEASFDlplfss--gntercTLQVCVMHRAlv 116  zebrafish
XP_002430461    7 AHVTILQAdnlliKGKNGTNNAFVVIELgkeIYRTSVKEnsgrSVVWNEECELKipki------gnkaSIVLTAQHRNsf 80   human body louse
NP_573313       7 CSVTVQRArglltKGKNGTNNCFVTIALgkeKYQTSVKDkaetSVNWNEECELKipdq------gnraELTLTCLHRNnl 80   fruit fly
XP_002732683   25 CRVTVHQArgllcKSRSHGHDAYVIMSIgrdKYQTSVVEkt-vHPHWDEQCDLHfsn--------tedNVELQVFHRNkl 95   Saccoglossus ...
Q6WKZ4         99 g-ldkFLGRAEVdlrdlhrdqgrrkTQWYKLkskpg---kkdkERGEIEVDIQ 147  human
XP_002126079   85 lesddFLGQVSVplsalnscdnkerARWYELngkks---gnkkERGEVEISFK 134  Ciona intestinalis
XP_421784      93 g-ldkFLGQVAIslndvfedkqrrkTEWFHLesrqg---krtkDRGEIKVNIQ 141  chicken
NP_001089307   92 g-ldkFLGQVCInlnnmfekkehrkTEWYKLeskqg---krnkERGELKVNIQ 140  African clawed frog
AAH57524      117 g-pdkTLGQASInllelqdntsrekTEWFKLlgktg---kadkDRGEVLLDIQ 165  zebrafish
XP_002430461   81 g-ldqFLGMVKIpldsfd--ktekrVKWFKLdgkpgknkdddkTRGKLEVQIG 130  human body louse
NP_573313      81 g-ideFLGQATLplnemd-vydrprAKWFKLeskpgk-ekknkERGELEVRIA 130  fruit fly
XP_002732683   96 l--ddFLGYVAIpirdie-fhgipiRRWHKLhnkrg--kkdakERGEIEVTVS 143  Saccoglossus kowalevskii
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