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List of -TEMs -PEMs -NEMs

TEMs TEM1 TEM2 TEM3 TEM4 TEM5 TEM6 TEM7 TEM8 TEM9 TEM10 TEM11 TEM12 TEM13 TEM14 TEM15 TEM16 TEM17 TEM18 TEM19 TEM20 TEM21_1 TEM21_2 TEM22 TEM23 TEM24 TEM25 TEM26 TEM27 TEM28 TEM29 TEM30 TEM31_1 TEM31_2 TEM32 TEM33 TEM34 TEM35 TEM36 TEM37 TEM38 TEM39 TEM40 TEM41 TEM42 TEM43 TEM44 TEM45 TEM46

Summary -Overview of TEMs -extracellular TEMs -intrac. & membrane TEMs -TEM tissue distribution

Supplementary -SAGE -Seq.analysis Methods

FAQ

Tumor Endothelial Marker Report: TEM21_2 (formin family member)

	TEM domain structure

	TEM Sequence Analysis

name	from	to	source/E	description
LCR	1	36	SEG	Proline-rich. Blastp and conclusions derived from the potential Takifugu orthologue hint on the possibility that poly-proline FH1 is to be expected in the further N-terminus.
FH2	36	467	PFAM, E = 8.9e-143	The region is highly alpha-helical in composition (93.7 %) with reliable coiled coils predicted for 345-372, 394-426. FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. A proline-rich FH1 domain usually found N-terminally of FH2 mediates these interactions.
500

	Remarks

• RELIABILITY: The incomplete protein 7328133|emb|CAB82400.1 was extended N-terminally using the genomic DNA. The protein-sequence of the Takifugu homologue gb|AAC34395.1 was used as a reference. View the BlastX of a segment of the working draft sequence gi|11433881 to see how the protein was extended. As the genomic sequence is an incomplete draft, the possibility of extension was limited.

• CLASSIFICATION: Proposed member of the Formin/Diaphanous family of proteins.

• DOMAIN ARCHITECTURE: The majority of the protein-sequence has been translated from a cDNA and is fragmentary with the N-terminus missing. The fragment contains a FH2 domain spanning over almost the complete length of the protein. As proteins of the formin family are usually found to contain a FH1 further N-terminal and the FH2 in the extreme carboxy-terminus, assumptions can be made on the missing N-terminal part of the sequence. Suggestions on the potential N-terminus of the sequence might be derived from gb|AAC34395.1, a homologue in fish with 88% sequence-identity. The protein was analyzed by a suite of single sequence analysis techniques. A polyproline region similar to the FH1 domain in other formins is found at position 520-575 of the proposed Takifugu-sequence and a FH3 domain is potentially located further N-terminally (see psi-blast of gb|AAC34395.1).

• FUNCTION: The closest related studied protein is the formin-related gene in leukocytes [Mus musculus] ref|NP_062653.1 (with 54% identity). The FRL has been shown to bind:
  • Rac at its N-terminal region including the FH3 domain
  • and profilin at the FH1 domain.
  Its functional role is proposed to be the control of reorganization of the actin cytoskeleton during cell adhesion to fibronectin and cell migration. An involvment in cell survival has been noted.
  Formin proteins are thought of as Rho downstream effector. The interaction of N-terminal of formin proteins with activated small GTPases, induces the interaction of the FH1 domain with profilin (an actin-binding protein). As a consequence, actin-polymerization is induced in the cell.

	Sequence Information

TEM	TEM21_2
Reliability of Gen2Tag mapping	Cid->tag (Hs.198182) frequency: tem21_2: CATG-TACCACCTCC=1/1 (cDNA) tem21_2: CATG-TACCACCTCC=1/3 (EST oriented)
Analysis	BlastP against nr   Output Created by a Suite of Single Sequence Analysis Techniques SIMILAR GENES in: C. elegans, Fugu rubripes, H. sapiens, M. musculus, S.cerevisiae
Protein Description	SEQ.SOURCE: gi|7328133|emb|CAB82400.1| hypothetical N-terminally extended with about 76aa making use of the genomic sequence
Protein Sequence	LPPPPDKCPPAPPLPGAAPSVVLTVPPGLSAIRIKKPPPIKTKFRLPVFNWTALKPNQIPSGTVFSELDD EKILEDKFEELFKTKAQGPALDLICSKNKTAQKAASKVTLLEANRAKNLAITLRKAGRSAEEICRAIHTF DLQTLPVDFVECLMRFLPTEAEVKLLRQYERERQPLEELAAEDRFMLLFSKVERLTQRMAGMAFLGNFQD NLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKMTL LHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNSVLRNFLSTNE GKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEVMREKQLA QEAKKLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEGKDGTIEDIITVLKSVPFTARTAKRGSRFFC DAAHHDESNC
SAGE-Tag	CATG-TACCACCTCCC
EST/cluster Description	UNIGEN CLUSTER: UniGene Cluster Hs.198182 SEQ.SOURCE: gi|7328132|emb|AL162062.1|HSM802593 cDNA DKFZp762B245 MARKINGS: TEM21_2 Tag in red
EST/cluster Sequence	GATAAGTTTGAAGAATTATTCAAGACAAAAGCGCAGGGCCCTGCCCTTGACCTCATCTGCTCCAAAAACA AGACAGCGCAAAAAGCTGCCAGCAAGGTGACTCTGTTGGAAGCCAATCGTGCCAAGAACCTGGCCATCAC CCTACGCAAGGCTGGCCGCTCGGCTGAGGAGATCTGCAGGGCCATTCATACGTTTGACTTGCAGACACTA CCTGTGGACTTCGTGGAGTGCCTGATGCGCTTCCTGCCCACAGAGGCTGAGGTAAAGCTGCTGCGGCAAT ATGAGCGGGAGCGGCAGCCCCTGGAGGAGTTGGCAGCTGAGGACCGCTTCATGCTGCTCTTCAGCAAGGT GGAACGGTTGACCCAGCGAATGGCTGGCATGGCCTTCCTGGGGAACTTCCAGGATAACCTGCAGATGCTC ACACCGCAACTCAATGCCATCATTGCGGCGTCCGCTTCCGTCAAGTCTTCACAGAAGCTGAAGCAGATGT TGGAGATCATACTTGCACTGGGGAACTACATGAACAGCAGCAAGCGGGGAGCTGTGTATGGCTTCAAGCT CCAGAGCCTGGATCTGCTGCTGGATACCAAGTCCACTGACCGGAAGATGACACTGCTTCATTTCATCGCC TTGACAGTGAAGGAGAAATACCCAGACCTGGCTAACTTCTGGCATGAGCTGCACTTTGTTGAGAAGGCTG CAGCAGTGTCCCTGGAGAACGTGCTGCTGGACGTGAAGGAGCTGGGCCGGGGCATGGAGCTGATTCGGCG TGAGTGCAGCATCCATGACAACAGCGTCCTCCGGAACTTCCTCAGTACCAATGAAGGCAAACTAGACAAG CTCCAGCGGGACGCCAAGACGGCTGAGGAGGCCTACAATGCAGTTGTGCGCTACTTTGGCGAGAGTCCCA AGACTACACCTCCTTCTGTATTCTTCCCAGTATTTGTCCGATTCATTCGTTCTTACAAGGAAGCAGAACA AGAGAATGAAGCCCGCAAGAAGCAGGAGGAGGTAATGCGGGAGAAGCAGCTGGCTCAGGAAGCCAAGAAA CTGGATGCCAAGACCCCATCCCAGCGGAACAAGTGGCAACAGCAGGAGTTAATAGCAGAGTTGAGGCGGC GCCAGGCCAAGGAACACCGGCCTGTTTATGAGGGGAAGGATGGTACCATCGAGGACATCATCACAGTGCT GAAGAGTGTCCCTTTCACGGCCCGTACTGCCAAGCGGGGCTCACGCTTCTTCTGTGATGCAGCCCACCAT GATGAGTCAAACTGTTAGCCCCCAAGGTTGGGGCCCGACAGGCCTCCACTGCCAGCCTATGGTTGTTCGC CACCAAGCCAGGAGTGCTGCACCGCCCAGTGGTCCCCCTCGGGCTCCAGGCCCCCACTGAGACCCTCTCG GAGGCAGAAGCACTTCACCCCTCAGAGTCCTACAAGTCCAACCAGTGGACCTGGAATTGGCCAAGGGCTC AGGAGAGGGCTGTGTTGCTCTCTCAACCATGTCCGCCCCAGCTCTTGAGGCTGGATCTTTCTACTTGTGC CACTATGGGCACTAGGTCTGTAGGTCCCTGGTGCTTCCAGTACTGCACTTTGCCCCCAAGGTCTTTGACT TCATTTCCTGAAGGGTCACCAAGGGTCAGCTCAGGGCTAGGAAAAACCATTTCCAGCCTTAGCCTAAACA GGGCACATAGATCTCTCCCACTAGAGCCCAGAGGGATGAGAGGAGAGAGCAACTGTTCTTTCTTTTTTTT TCCCTTCCTTTTTGCAGGCCCATGGTCAGCTCTGGTCTAGATGTATCTAGGCTTAGGGAGCCCTGGGACC CTGCCAGTCTCAGTTCATCTCTTACCAGGAGCAAGGCCCTCTGAAGCATGGGCCGTGCCAGCTGTGCCCT AGTGATAAGGGTAAGAGGAGAGATGTCAGGCTCACTGCCCTTATTTCTCTGCCCATTTCATTCTAGGCTC ACACTGTCCTTGTCAAGGTGGGCAGAAGAGCAGAGGTCTTCTCTGCACCAACCACTCTCTGCAGATGGCT GGAGAAAGGGTGTGCCAACTCTTCACCTTCTTTCCTCAGCTACGGTTTTTTTTTTTTTTTTTTTTTTTGG CAGGGGACAAGGAGCATGGTGGTCTTGGCTATTTGCTTACCTTCCCGTTTCTCCTCTGCCCCTGGAAGGG AATGTGGGGGCCCACTTTTTTGTACATGTACCACCTCCCTTTCCTCTTACTGTACATAAACCTCAGACTC TCCCCCTCTCAACAAAGGCTTGATGCACCAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAGGGGGGGCC
Genomic Sequence Description	chromosome 12 working draft sequence segment
Genomic Sequence

	Literature

PubMed: 20414696

FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages. Yayoshi-Yamamoto S, Taniuchi I, Watanabe T. Mol Cell Biol 2000 Sep;20(18):6872-81